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Conserved domains on  [gi|34147958|gb|AAQ62556|]
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Cps2D [Actinobacillus pleuropneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
 513-879 2.53e-92

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


:

Pssm-ID: 441491  Cd Length: 369  Bit Score: 302.30  E-value: 2.53e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  513 YSEYYNVLKIKDKTILYESFSGQGMSCNPYALFLYLLNHqeYKSWTHIWVVNNidniSSEYKKQHNIIFVSRGSDSYLRY 592
Cdd:COG1887   10 YYRLSRLLPVKKNIILFESRNGRSYSDNPKALFEYLRKN--HPDYEVVWVVDD----DSKRLPKEGVKVVKRGSLKYLYA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  593 LATAKVLINNSN--FPPYFIRKPEQKFLSTWHGTPFKTLGRDMEGRFfeHKNLTRNIFQSTHLLSPNAHTSKILYDRHEI 670
Cdd:COG1887   84 LARAKYLVSNHYfpFPSYFRKRKGQKYVQLWHGTPLKKIGLDDPPRY--LKRVLREYRNWDYLLSSSEESTEIFRRAFGY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  671 KEiytGKLIESGYPRID-MTLSLTEEEKLELREKLGVLNNEKLVFYAPTWRGTHGDIEFDYDKlksDLNKLSKL--KGAK 747
Cdd:COG1887  162 PE---GEVLETGYPRNDvLFDADREELREELRERLGIPEDKKVILYAPTWRDDEDNFDDYLDL---DLERLAELlgDDYV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  748 VIFRGHSLLQEALSKINLD-ITVAPDELDTNKILGVTDILITDYSSVLFDYLPTLKPLVLYMYDIKEYTEERGLYFS-EN 825
Cdd:COG1887  236 LLVRLHPFVKDSLDEKYSDrIIDVSDYPDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRDERGFYFDyEE 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34147958  826 ELPGEKCYNIDELVKTLTYLLENNITSVSVEDNKVAEFAPHDDGNVSEKVINAL 879
Cdd:COG1887  316 DAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 900-1286 2.88e-72

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


:

Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 245.35  E-value: 2.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  900 LLIYGGPFMGNGITTSVINLIANIDRSKYTITLVIDPGSiekevgrliqfeklpqdinvvarvgrMDMDLEERYIHglNN 979
Cdd:cd03811    2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDE--------------------------GDLDKQLNGDV--KL 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  980 QHYELQSSVAQDILWNSWEKEYQRIFGNAKFDSLIQFEGYNRFWSGVFTSIKNKKSsIYMHNSMEEEYRLKYPYLKsIFY 1059
Cdd:cd03811   54 IRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISFLGFATYIVAKLAAARSKVI-AWIHSSLSKLYYLKKKLLL-KLK 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1060 YCSLADKVISVSELTmklnQDKLSDRFNIPLSKFDYSDNLQQPEKIKVLARDELLeqdkaYFNTEDKVFLTIGRLSIEKD 1139
Cdd:cd03811  132 LYKKADKIVCVSKGI----KEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPIL-----NEPEDGPVILAVGRLDPQKG 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1140 HAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEA 1219
Cdd:cd03811  203 HDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEA 282

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147958 1220 MILEKMIIATDIVGSRSALE-GRSGYLVENSVSGLEKGMLDYISGSLPLVT-YDINEYQKQAINKFYSI 1286
Cdd:cd03811  283 MALGTPVVSTDCPGPREILDdGENGLLVPDGDAAALAGILAALLQKKLDAAlRERLAKAQEAVFREYTI 351
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 243-480 2.06e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 86.71  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEA 322
Cdd:COG2956   23 QPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  323 LSLKQK-PEWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKASKMY---LKLRKNTELAL 398
Cdd:COG2956  103 LELDPDdAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCEL-AELYLEQGDYDEAIEALekaLKLDPDCARAL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  399 KNKI---HNKEAVEKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRSEilNSLGYYRLAFVQLKQN 475
Cdd:COG2956  182 LLLAelyLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDP--SDDLLLALADLLERKE 259


                 ....*
gi 34147958  476 KYEEA 480
Cdd:COG2956  260 GLEAA 264
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 18-359 2.47e-17

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 83.63  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAyhyisiatnlapeilqwqvqlrqsevrIRL 97
Cdd:COG2956   12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRA---------------------------IRI 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   98 kkHKKksvigktsvhkiveeqqkinideikritsssandiaeqiiidALEKEPENASLYAELASFQNKQNKLWQSVDSWG 177
Cdd:COG2956   65 --HQK------------------------------------------LLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQA 257
Cdd:COG2956  101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERL--LKLGPENAHAYCELAELYLEQG-----DYDEAIEALEKALKL 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  258 DRK-LRAKdFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQKPEWRFRLG 336
Cdd:COG2956  174 DPDcARAL-LLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALA 252

                        330       340
                 ....*....|....*....|...
gi 34147958  337 FVQERQNKFDQATINYEQAATER 359
Cdd:COG2956  253 DLLERKEGLEAALALLERQLRRH 275
 
Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
 513-879 2.53e-92

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 441491  Cd Length: 369  Bit Score: 302.30  E-value: 2.53e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  513 YSEYYNVLKIKDKTILYESFSGQGMSCNPYALFLYLLNHqeYKSWTHIWVVNNidniSSEYKKQHNIIFVSRGSDSYLRY 592
Cdd:COG1887   10 YYRLSRLLPVKKNIILFESRNGRSYSDNPKALFEYLRKN--HPDYEVVWVVDD----DSKRLPKEGVKVVKRGSLKYLYA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  593 LATAKVLINNSN--FPPYFIRKPEQKFLSTWHGTPFKTLGRDMEGRFfeHKNLTRNIFQSTHLLSPNAHTSKILYDRHEI 670
Cdd:COG1887   84 LARAKYLVSNHYfpFPSYFRKRKGQKYVQLWHGTPLKKIGLDDPPRY--LKRVLREYRNWDYLLSSSEESTEIFRRAFGY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  671 KEiytGKLIESGYPRID-MTLSLTEEEKLELREKLGVLNNEKLVFYAPTWRGTHGDIEFDYDKlksDLNKLSKL--KGAK 747
Cdd:COG1887  162 PE---GEVLETGYPRNDvLFDADREELREELRERLGIPEDKKVILYAPTWRDDEDNFDDYLDL---DLERLAELlgDDYV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  748 VIFRGHSLLQEALSKINLD-ITVAPDELDTNKILGVTDILITDYSSVLFDYLPTLKPLVLYMYDIKEYTEERGLYFS-EN 825
Cdd:COG1887  236 LLVRLHPFVKDSLDEKYSDrIIDVSDYPDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRDERGFYFDyEE 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34147958  826 ELPGEKCYNIDELVKTLTYLLENNITSVSVEDNKVAEFAPHDDGNVSEKVINAL 879
Cdd:COG1887  316 DAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 522-881 4.93e-78

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 261.90  E-value: 4.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    522 IKDKTILYESFSGQGMSCNPYALFLYLLNhqEYKSWTHIWVVNNIDNISSeykkQHNIIFVSRGSDSYLRYLATAKVLIN 601
Cdd:pfam04464    2 LDPNLVLFESFWGRGYSDNPKAIYEYLRE--LAPGYRIVWVVKKDHSARL----PKGVPVVVRNSFRYLYLLLRAKYLVS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    602 NSNFPPYFIRKPEQKFLSTWHGTPFKTLGRDMEGR--FFEHKNLTRNIFQSTHLLSPNAHTSKILYDRHEIKEiytGKLI 679
Cdd:pfam04464   76 NSNFPLYVVKRKNQVYLQTWHGTPLKHMGLDILEVpmANTGQNFLRNVDRWDYLISANPHSTNIFARAFNIDK---ERIL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    680 ESGYPRIDMTLSLTEEEKLELREKLGVLNNEKLVFYAPTWRGT-HGDIEFDYDKLKSDLNKLSKLKG--AKVIFRGHSLL 756
Cdd:pfam04464  153 ETGYPRNDVLFNANNEDVQRIRERLGIPLGKKVILYAPTWRDDeRGSIGSYRFELLIDLERLAFALGndYVILLKMHPLI 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    757 QEALSKINLD--ITVAPDELDTNKILGVTDILITDYSSVLFDYLPTLKPLVLYMYDIKEYTEERGLYFS-ENELPGEKCY 833
Cdd:pfam04464  233 QNNIDIFESSgyVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLETYSATRGFYLDyESEAPGPVVE 312

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 34147958    834 NIDELVKTLTYLLENNITSVSVEDNKVAEFAPHDDGNVSEKVINALFS 881
Cdd:pfam04464  313 TFDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLIFL 360
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 900-1286 2.88e-72

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 245.35  E-value: 2.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  900 LLIYGGPFMGNGITTSVINLIANIDRSKYTITLVIDPGSiekevgrliqfeklpqdinvvarvgrMDMDLEERYIHglNN 979
Cdd:cd03811    2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDE--------------------------GDLDKQLNGDV--KL 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  980 QHYELQSSVAQDILWNSWEKEYQRIFGNAKFDSLIQFEGYNRFWSGVFTSIKNKKSsIYMHNSMEEEYRLKYPYLKsIFY 1059
Cdd:cd03811   54 IRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISFLGFATYIVAKLAAARSKVI-AWIHSSLSKLYYLKKKLLL-KLK 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1060 YCSLADKVISVSELTmklnQDKLSDRFNIPLSKFDYSDNLQQPEKIKVLARDELLeqdkaYFNTEDKVFLTIGRLSIEKD 1139
Cdd:cd03811  132 LYKKADKIVCVSKGI----KEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPIL-----NEPEDGPVILAVGRLDPQKG 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1140 HAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEA 1219
Cdd:cd03811  203 HDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEA 282

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147958 1220 MILEKMIIATDIVGSRSALE-GRSGYLVENSVSGLEKGMLDYISGSLPLVT-YDINEYQKQAINKFYSI 1286
Cdd:cd03811  283 MALGTPVVSTDCPGPREILDdGENGLLVPDGDAAALAGILAALLQKKLDAAlRERLAKAQEAVFREYTI 351
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
1126-1248 7.39e-27

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 107.21  E-value: 7.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   1126 KVFLTIGRLSIEKDHAK-LINSFANVVKKYPKTQLLIIGDGSLRYpLVQQIKqlGLEKNVHLLGLRANPFPLLKKADCFI 1204
Cdd:pfam13692    2 PVILFVGRLHPNVKGVDyLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAA--GLEDRVIFTGFVEDLAELLAAADVFV 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 34147958   1205 LPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALEGRSGYLVEN 1248
Cdd:pfam13692   79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPP 122
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 1110-1246 8.81e-20

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 92.86  E-value: 8.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   1110 RDELLEQDkaYFNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQ----LLIIGDGSLRYPLVQQIKQLGLEKNVH 1185
Cdd:TIGR03088  181 RSPILPPD--FFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGAerlrLVIVGDGPARGACEQMVRAAGLAHLVW 258

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34147958   1186 LLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDiVGSRSAL--EGRSGYLV 1246
Cdd:TIGR03088  259 LPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATA-VGGNPELvqHGVTGALV 320
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 243-480 2.06e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 86.71  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEA 322
Cdd:COG2956   23 QPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  323 LSLKQK-PEWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKASKMY---LKLRKNTELAL 398
Cdd:COG2956  103 LELDPDdAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCEL-AELYLEQGDYDEAIEALekaLKLDPDCARAL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  399 KNKI---HNKEAVEKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRSEilNSLGYYRLAFVQLKQN 475
Cdd:COG2956  182 LLLAelyLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDP--SDDLLLALADLLERKE 259


                 ....*
gi 34147958  476 KYEEA 480
Cdd:COG2956  260 GLEAA 264
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 18-359 2.47e-17

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 83.63  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAyhyisiatnlapeilqwqvqlrqsevrIRL 97
Cdd:COG2956   12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRA---------------------------IRI 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   98 kkHKKksvigktsvhkiveeqqkinideikritsssandiaeqiiidALEKEPENASLYAELASFQNKQNKLWQSVDSWG 177
Cdd:COG2956   65 --HQK------------------------------------------LLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQA 257
Cdd:COG2956  101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERL--LKLGPENAHAYCELAELYLEQG-----DYDEAIEALEKALKL 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  258 DRK-LRAKdFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQKPEWRFRLG 336
Cdd:COG2956  174 DPDcARAL-LLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALA 252

                        330       340
                 ....*....|....*....|...
gi 34147958  337 FVQERQNKFDQATINYEQAATER 359
Cdd:COG2956  253 DLLERKEGLEAALALLERQLRRH 275
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1178-1262 3.49e-12

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 64.63  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1178 LGLEKNVHLLgLRAnpfpLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLVE-NSVSGLEK 1255
Cdd:COG0438    4 LVPRKGLDLL-LEA----LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdGETGLLVPpGDPEALAE 78


                 ....*..
gi 34147958 1256 GMLDYIS 1262
Cdd:COG0438   79 AILRLLE 85
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 18-480 5.23e-12

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 70.50  E-value: 5.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEILQwqvqlrqsevrirl 97
Cdd:TIGR02917  265 YLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQ-------------- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     98 kkhkkksvigktsvhkiveeqqkinideIKRItsssandiaeqiiidalekepenaslyaeLASFQNKQNKLWQSVDSWG 177
Cdd:TIGR02917  331 ----------------------------ARRL-----------------------------LASIQLRLGRVDEAIATLS 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLsmKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQA 257
Cdd:TIGR02917  354 PALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATEL--DPENAAARTQLGISKLSQG-----DPSEAIADLETAAQL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    258 DRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQK-PEWRFRLG 336
Cdd:TIGR02917  427 DPELGRADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDfFPAAANLA 506

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    337 FVQERQNKFDQATINYEQAATERKQYTPY------WFYRSAYTLEKQGLYEKASKmylklRKNTELALK-----NKIHNK 405
Cdd:TIGR02917  507 RIDIQEGNPDDAIQRFEKVLTIDPKNLRAilalagLYLRTGNEEEAVAWLEKAAE-----LNPQEIEPAlalaqYYLGKG 581

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147958    406 EAvEKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAeLAYYQAVSRSEILNSLGYYRLAFVQLKQNKYEEA 480
Cdd:TIGR02917  582 QL-KKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKA-VSSFKKLLALQPDSALALLLLADAYAVMKNYAKA 654
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
1130-1249 8.87e-09

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 59.71  E-value: 8.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  1130 TIG---RLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILP 1206
Cdd:PRK15490  400 TIGgvfRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILF 479

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 34147958  1207 SNHEGQPMTLFEAMILEKMIIATDIVGSRSA-LEGRSGYLVENS 1249
Cdd:PRK15490  480 SRYEGLPNVLIEAQMVGVPVISTPAGGSAECfIEGVSGFILDDA 523
MamA NF040959
magnetosome protein MamA; Magnetosomes are special lipid-bound organelles that comprise ...
 153-348 4.98e-07

magnetosome protein MamA; Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family typically contain five tetra-trico-peptide repeat (TPR) motifs. Based on structural analyses, MamA forms a large homooligomer through self-recognition to regulate protein-protein interaction in magnetosomes.


Pssm-ID: 468889 [Multi-domain]  Cd Length: 204  Bit Score: 51.61  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   153 ASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLsmkenlsdlyfrlgfv 232
Cdd:NF040959   37 AKMYRNKGISHAKKGRYDKAVRYLEQVARIDPDDVEALYRLGVAYLKTGQYDRAIKVLEKVLSL---------------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   233 nenqGHDNeidlevAKQAYGLAIQAdrkLRAKDFGigvfhehrrdwgRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQF 312
Cdd:NF040959  101 ----APDH------VKAAYRKGVAL---LKIKDYE------------KAVEDLEEALEEKPDNFNLNYRLGLALDGLGQY 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 34147958   313 GQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQA 348
Cdd:NF040959  156 DKAIEAFQKALELDpNEIKYHQAIGFMYVQKGDHETA 192
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 18-67 1.82e-04

tol-pal system protein YbgF; Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction.


Pssm-ID: 188247 [Multi-domain]  Cd Length: 117  Bit Score: 42.27  E-value: 1.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 34147958     18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSN---FKLGMCFFKQGVWDKA 67
Cdd:TIGR02795   41 YWLGEAYYAQGDYADAAKAFLAVVKKYPKSPKAPdalLKLGMSLQELGDKEKA 93
 
Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
 513-879 2.53e-92

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 441491  Cd Length: 369  Bit Score: 302.30  E-value: 2.53e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  513 YSEYYNVLKIKDKTILYESFSGQGMSCNPYALFLYLLNHqeYKSWTHIWVVNNidniSSEYKKQHNIIFVSRGSDSYLRY 592
Cdd:COG1887   10 YYRLSRLLPVKKNIILFESRNGRSYSDNPKALFEYLRKN--HPDYEVVWVVDD----DSKRLPKEGVKVVKRGSLKYLYA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  593 LATAKVLINNSN--FPPYFIRKPEQKFLSTWHGTPFKTLGRDMEGRFfeHKNLTRNIFQSTHLLSPNAHTSKILYDRHEI 670
Cdd:COG1887   84 LARAKYLVSNHYfpFPSYFRKRKGQKYVQLWHGTPLKKIGLDDPPRY--LKRVLREYRNWDYLLSSSEESTEIFRRAFGY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  671 KEiytGKLIESGYPRID-MTLSLTEEEKLELREKLGVLNNEKLVFYAPTWRGTHGDIEFDYDKlksDLNKLSKL--KGAK 747
Cdd:COG1887  162 PE---GEVLETGYPRNDvLFDADREELREELRERLGIPEDKKVILYAPTWRDDEDNFDDYLDL---DLERLAELlgDDYV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  748 VIFRGHSLLQEALSKINLD-ITVAPDELDTNKILGVTDILITDYSSVLFDYLPTLKPLVLYMYDIKEYTEERGLYFS-EN 825
Cdd:COG1887  236 LLVRLHPFVKDSLDEKYSDrIIDVSDYPDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRDERGFYFDyEE 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34147958  826 ELPGEKCYNIDELVKTLTYLLENNITSVSVEDNKVAEFAPHDDGNVSEKVINAL 879
Cdd:COG1887  316 DAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 522-881 4.93e-78

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 261.90  E-value: 4.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    522 IKDKTILYESFSGQGMSCNPYALFLYLLNhqEYKSWTHIWVVNNIDNISSeykkQHNIIFVSRGSDSYLRYLATAKVLIN 601
Cdd:pfam04464    2 LDPNLVLFESFWGRGYSDNPKAIYEYLRE--LAPGYRIVWVVKKDHSARL----PKGVPVVVRNSFRYLYLLLRAKYLVS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    602 NSNFPPYFIRKPEQKFLSTWHGTPFKTLGRDMEGR--FFEHKNLTRNIFQSTHLLSPNAHTSKILYDRHEIKEiytGKLI 679
Cdd:pfam04464   76 NSNFPLYVVKRKNQVYLQTWHGTPLKHMGLDILEVpmANTGQNFLRNVDRWDYLISANPHSTNIFARAFNIDK---ERIL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    680 ESGYPRIDMTLSLTEEEKLELREKLGVLNNEKLVFYAPTWRGT-HGDIEFDYDKLKSDLNKLSKLKG--AKVIFRGHSLL 756
Cdd:pfam04464  153 ETGYPRNDVLFNANNEDVQRIRERLGIPLGKKVILYAPTWRDDeRGSIGSYRFELLIDLERLAFALGndYVILLKMHPLI 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    757 QEALSKINLD--ITVAPDELDTNKILGVTDILITDYSSVLFDYLPTLKPLVLYMYDIKEYTEERGLYFS-ENELPGEKCY 833
Cdd:pfam04464  233 QNNIDIFESSgyVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLETYSATRGFYLDyESEAPGPVVE 312

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 34147958    834 NIDELVKTLTYLLENNITSVSVEDNKVAEFAPHDDGNVSEKVINALFS 881
Cdd:pfam04464  313 TFDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLIFL 360
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 900-1286 2.88e-72

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 245.35  E-value: 2.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  900 LLIYGGPFMGNGITTSVINLIANIDRSKYTITLVIDPGSiekevgrliqfeklpqdinvvarvgrMDMDLEERYIHglNN 979
Cdd:cd03811    2 ILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRDE--------------------------GDLDKQLNGDV--KL 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  980 QHYELQSSVAQDILWNSWEKEYQRIFGNAKFDSLIQFEGYNRFWSGVFTSIKNKKSsIYMHNSMEEEYRLKYPYLKsIFY 1059
Cdd:cd03811   54 IRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISFLGFATYIVAKLAAARSKVI-AWIHSSLSKLYYLKKKLLL-KLK 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1060 YCSLADKVISVSELTmklnQDKLSDRFNIPLSKFDYSDNLQQPEKIKVLARDELLeqdkaYFNTEDKVFLTIGRLSIEKD 1139
Cdd:cd03811  132 LYKKADKIVCVSKGI----KEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPIL-----NEPEDGPVILAVGRLDPQKG 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1140 HAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEA 1219
Cdd:cd03811  203 HDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEA 282

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147958 1220 MILEKMIIATDIVGSRSALE-GRSGYLVENSVSGLEKGMLDYISGSLPLVT-YDINEYQKQAINKFYSI 1286
Cdd:cd03811  283 MALGTPVVSTDCPGPREILDdGENGLLVPDGDAAALAGILAALLQKKLDAAlRERLAKAQEAVFREYTI 351
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 1022-1257 2.91e-33

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 132.72  E-value: 2.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1022 FWSGVFTSIKNKKSSIYM----HNSMEEEYRLKYPYLKSIFYYCSLADKVISVSE------LTMKLNQDKLSDRFN---I 1088
Cdd:cd03808   94 ILGRLAARLAGVPKVIYTvhglGFVFTEGKLLRLLYLLLEKLALLFTDKVIFVNEddrdlaIKKGIIKKKKTVLIPgsgV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1089 PLSKFDYSDNLQQPEKIkvlardelleqdkayfntedkVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLR 1168
Cdd:cd03808  174 DLDRFQYSPESLPSEKV---------------------VFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1169 YPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSA-LEGRSGYLVE 1247
Cdd:cd03808  233 NPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELvIDGVNGFLVP 312

                        250
                 ....*....|.
gi 34147958 1248 -NSVSGLEKGM 1257
Cdd:cd03808  313 pGDVEALADAI 323
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 900-1262 2.12e-28

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 118.41  E-value: 2.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  900 LLIYGGPFMGNGITTSVINLIANIDRSKYTITlvidpgsiekevgrliqfeklpqdinVVARVGRMDMDLEERYIHGLNN 979
Cdd:cd03801    4 LLSPELPPPVGGAERHVRELARALAARGHDVT--------------------------VLTPADPGEPPEELEDGVIVPL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  980 QHYELQSSVAQDILwnsweKEYQRIFGNAKFDsLIQFEGYNRFWSGVFTSIKNKKSSIY-MHNSMEEEYRL----KYPYL 1054
Cdd:cd03801   58 LPSLAALLRARRLL-----RELRPLLRLRKFD-VVHAHGLLAALLAALLALLLGAPLVVtLHGAEPGRLLLllaaERRLL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1055 KSIFYYCSLADKVISVSELTmklnQDKLSDRFNIPlskfdysdnlqqPEKIKV------LARDELLEQDKAYFNTEDKVF 1128
Cdd:cd03801  132 ARAEALLRRADAVIAVSEAL----RDELRALGGIP------------PEKIVVipngvdLERFSPPLRRKLGIPPDRPVL 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1129 LTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSlryPLVQQIKQ--LGLEKNVHLLGLRANP--FPLLKKADCFI 1204
Cdd:cd03801  196 LFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDG---PLRAELEEleLGLGDRVRFLGFVPDEelPALYAAADVFV 272

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1205 LPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALEGRSGYLV--ENSVSGLEKGMLDYIS 1262
Cdd:cd03801  273 LPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVvpPDDVEALADALLRLLA 332
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
1126-1248 7.39e-27

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 107.21  E-value: 7.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   1126 KVFLTIGRLSIEKDHAK-LINSFANVVKKYPKTQLLIIGDGSLRYpLVQQIKqlGLEKNVHLLGLRANPFPLLKKADCFI 1204
Cdd:pfam13692    2 PVILFVGRLHPNVKGVDyLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAA--GLEDRVIFTGFVEDLAELLAAADVFV 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 34147958   1205 LPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALEGRSGYLVEN 1248
Cdd:pfam13692   79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPP 122
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 1065-1248 1.48e-26

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 112.80  E-value: 1.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1065 DKVISVSE--LTMKLNQDKLSDRFNIPLSKFDySDNLQQPEKIKVLARDELLEQDKAYfntedkVFLTIGRLSIEKDHAK 1142
Cdd:cd03807  135 PATVANSSavAEFHQEQGYAKNKIVVIYNGID-LFKLSPDDASRARARRRLGLAEDRR------VIGIVGRLHPVKDHSD 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1143 LINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMIL 1222
Cdd:cd03807  208 LLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMAC 287

                        170       180
                 ....*....|....*....|....*.
gi 34147958 1223 EKMIIATDIVGSRSALEGRSGYLVEN 1248
Cdd:cd03807  288 GLPVVATDVGGAAELVDDGTGFLVPA 313
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 1119-1262 6.49e-25

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 107.71  E-value: 6.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1119 AYFNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLK 1198
Cdd:cd03820  175 PSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYA 254

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34147958 1199 KADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSAL--EGRSGYLVEN-SVSGLEKGMLDYIS 1262
Cdd:cd03820  255 NSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIieDGENGLLVPNgDVDALAEALLRLME 321
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 1124-1262 6.82e-25

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 102.35  E-value: 6.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   1124 EDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFP--LLKKAD 1201
Cdd:pfam00534    1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLpeLLKIAD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34147958   1202 CFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSAL-EGRSGYLVE-NSVSGLEKGMLDYIS 1262
Cdd:pfam00534   81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkDGETGFLVKpNNAEALAEAIDKLLE 143
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 1088-1239 2.11e-22

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 100.60  E-value: 2.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1088 IPLSKFDYSDNLQQpeKIKvlardelleqDKAYFNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSL 1167
Cdd:cd04951  163 IDLNKFKKDINVRL--KIR----------NKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPL 230

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34147958 1168 RYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE 1239
Cdd:cd04951  231 RNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVG 302
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 1124-1246 2.23e-21

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 94.39  E-value: 2.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1124 EDKVFltIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFP---LLKKA 1200
Cdd:cd01635  111 ADKVS--VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVlelLLAAA 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 34147958 1201 DCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLV 1246
Cdd:cd01635  189 DVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVdGENGLLV 235
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 1040-1246 4.15e-21

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 96.27  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1040 HNSMEEEYRLKYPYLKSIFYycslADKVISVSELTmklnQDKLSDRFNIPlskfdysdnlqqPEKIKVLAR--------D 1111
Cdd:cd03819  107 HGSYLATYHPKDFALAVRAR----GDRVIAVSELV----RDHLIEALGVD------------PERIRVIPNgvdtdrfpP 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1112 ELLEQDKAYFNTEDKVF--LTIGRLSIEKDHAKLINSfANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGL 1189
Cdd:cd03819  167 EAEAEERAQLGLPEGKPvvGYVGRLSPEKGWLLLVDA-AAELKDEPDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGF 245

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34147958 1190 RANPFPLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLV 1246
Cdd:cd03819  246 REDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVhGRTGLLV 303
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 1088-1221 4.63e-20

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 93.51  E-value: 4.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1088 IPLSKFDYSDNLQQPEKIKVLARDELleqdkayfntedkVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSL 1167
Cdd:cd03812  167 IDIEKYKFNKEKRRKRRKLLILEDKL-------------VLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGEL 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34147958 1168 RYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMI 1221
Cdd:cd03812  234 KEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQA 287
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 1110-1246 8.81e-20

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 92.86  E-value: 8.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   1110 RDELLEQDkaYFNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQ----LLIIGDGSLRYPLVQQIKQLGLEKNVH 1185
Cdd:TIGR03088  181 RSPILPPD--FFADESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGAerlrLVIVGDGPARGACEQMVRAAGLAHLVW 258

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34147958   1186 LLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDiVGSRSAL--EGRSGYLV 1246
Cdd:TIGR03088  259 LPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATA-VGGNPELvqHGVTGALV 320
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 1126-1247 2.81e-19

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 91.29  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1126 KVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGlranPFP------LLKK 1199
Cdd:cd03798  201 FVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTG----RLPheqvpaYYRA 276

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 34147958 1200 ADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLVE 1247
Cdd:cd03798  277 CDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGdPETGLLVP 325
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 243-480 2.06e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 86.71  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEA 322
Cdd:COG2956   23 QPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  323 LSLKQK-PEWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKASKMY---LKLRKNTELAL 398
Cdd:COG2956  103 LELDPDdAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCEL-AELYLEQGDYDEAIEALekaLKLDPDCARAL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  399 KNKI---HNKEAVEKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRSEilNSLGYYRLAFVQLKQN 475
Cdd:COG2956  182 LLLAelyLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDP--SDDLLLALADLLERKE 259


                 ....*
gi 34147958  476 KYEEA 480
Cdd:COG2956  260 GLEAA 264
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 266-513 2.35e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 86.71  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  266 FGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSL-KQKPEWRFRLGFVQERQNK 344
Cdd:COG2956   12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERdPDRAEALLELAQDYLKAGL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  345 FDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKASKMYLKLRKNT-----------ELALKNKiHNKEAVEKLIF 413
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRLL-AEIYEQEGDWEKAIEVLERLLKLGpenahaycelaELYLEQG-DYDEAIEALEK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  414 ILnkkhQYDASSAESWFDLGTYYEFLNDWEQAeLAYYQAVSRSEILNSLGYYRLAFVQLKQNKYEEACENFRnyRVMQRP 493
Cdd:COG2956  170 AL----KLDPDCARALLLLAELYLEQGDYEEA-IAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLR--KALELD 242

                        250       260
                 ....*....|....*....|....*
gi 34147958  494 HGVNE-----DYLSKDIGFAEAASY 513
Cdd:COG2956  243 PSDDLllalaDLLERKEGLEAALAL 267
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 18-359 2.47e-17

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 83.63  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAyhyisiatnlapeilqwqvqlrqsevrIRL 97
Cdd:COG2956   12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRA---------------------------IRI 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   98 kkHKKksvigktsvhkiveeqqkinideikritsssandiaeqiiidALEKEPENASLYAELASFQNKQNKLWQSVDSWG 177
Cdd:COG2956   65 --HQK------------------------------------------LLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQA 257
Cdd:COG2956  101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERL--LKLGPENAHAYCELAELYLEQG-----DYDEAIEALEKALKL 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  258 DRK-LRAKdFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQKPEWRFRLG 336
Cdd:COG2956  174 DPDcARAL-LLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALA 252

                        330       340
                 ....*....|....*....|...
gi 34147958  337 FVQERQNKFDQATINYEQAATER 359
Cdd:COG2956  253 DLLERKEGLEAALALLERQLRRH 275
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 957-1262 8.24e-17

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 83.57  E-value: 8.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  957 NVVARVGRMDMDLEERYIHGLNNQHYELQSSVAQDILWNSWEKEYQRIFGNAKFD-SLIQFEGYNRFWSGVFT---SIKN 1032
Cdd:cd03809   22 ELLKALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQiLLPKKDKPDLLHSPHNTaplLLKG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1033 KKSSIYMHNSMEEEYRLKYPYLKSIFYY------CSLADKVISVSELTmklnQDKLSDRFNIPlskfdysdnlqqPEKIK 1106
Cdd:cd03809  102 CPQVVTIHDLIPLRYPEFFPKRFRLYYRlllpisLRRADAIITVSEAT----RDDIIKFYGVP------------PEKIV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1107 V--LARD------ELLEQDKAYFNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIG-DGSLRYPLVQQIKQ 1177
Cdd:cd03809  166 VipLGVDpsffppESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGgKGWEDEELLDLVKK 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1178 LGLEKNVHLLG------LRAnpfpLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIvgsrSALE---GRSGYLV-E 1247
Cdd:cd03809  246 LGLGGRVRFLGyvsdedLPA----LYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNI----SVLPevaGDAALYFdP 317

                        330
                 ....*....|....*
gi 34147958 1248 NSVSGLEKGMLDYIS 1262
Cdd:cd03809  318 LDPESIADAILRLLE 332
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
216-469 1.17e-16

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 81.21  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  216 LSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNN 295
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLG-----RYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  296 PELLYRLGFAYDRNYQFGQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTL 374
Cdd:COG0457   76 AEALNNLGLALQALGRYEEALEDYDKALELDpDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL-GIAL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  375 EKQGLYEKASKMYLKLRKNTELALKNkihnkEAVEKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVS 454
Cdd:COG0457  155 EKLGRYEEALELLEKLEAAALAALLA-----AALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALAL 229

                        250
                 ....*....|....*
gi 34147958  455 RSEILNSLGYYRLAF 469
Cdd:COG0457  230 LLALRLAALALYQYR 244
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
146-323 3.31e-16

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 79.67  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  146 LEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDL 225
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQA--LELDPDDAEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  226 YFRLGFVNENQGhdneiDLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFA 305
Cdd:COG0457   79 LNNLGLALQALG-----RYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIA 153

                        170
                 ....*....|....*...
gi 34147958  306 YDRNYQFGQAENIYKEAL 323
Cdd:COG0457  154 LEKLGRYEEALELLEKLE 171
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 1128-1248 1.00e-15

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 80.04  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1128 FLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPS 1207
Cdd:cd04949  163 IITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTS 242

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 34147958 1208 NHEGQPMTLFEAMILEKMIIATDI-VGSRSALE-GRSGYLVEN 1248
Cdd:cd04949  243 QMEGFGLTLMEAIGHGLPVVSYDVkYGPSELIEdGENGYLIEK 285
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
289-488 1.47e-15

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 77.74  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  289 LEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQKPEW-RFRLGFVQERQNKFDQATINYEQAATERKQYTPYWF 367
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEaLYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  368 YRsAYTLEKQGLYEKASKMYLKlrkntelALknkihnkeaveklifilnkkhQYDASSAESWFDLGTYYEFLNDWEQAEL 447
Cdd:COG0457   81 NL-GLALQALGRYEEALEDYDK-------AL---------------------ELDPDDAEALYNLGLALLELGRYDEAIE 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 34147958  448 AYYQAVSRsEILNSLGYYRLAFVQLKQNKYEEACENFRNYR 488
Cdd:COG0457  132 AYERALEL-DPDDADALYNLGIALEKLGRYEEALELLEKLE 171
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 1115-1258 4.60e-15

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 78.47  E-value: 4.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1115 EQDKAYFNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKyPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGlranPF 1194
Cdd:cd03817  191 ERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTG----FV 265

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34147958 1195 P------LLKKADCFILPSNHEGQPMTLFEAM------ILEKMIIATDIVGsrsalEGRSGYLVENSVSGLEKGML 1258
Cdd:cd03817  266 PreelpeYYKAADLFVFASTTETQGLVYLEAMaaglpvVAAKDPAASELVE-----DGENGFLFEPNDETLAEKLL 336
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 1129-1263 5.17e-15

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 78.26  E-value: 5.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1129 LTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANP--FPLLKKADCFILP 1206
Cdd:cd03799  178 LTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEeiIEILDEADIFIAP 257

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147958 1207 S------NHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLV-ENSVSGLEKGMLDYISG 1263
Cdd:cd03799  258 SvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEdGVSGFLVpERDAEAIAEKLTYLIEH 322
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 136-390 5.61e-14

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 73.61  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  136 DIAEQIIIDALEKEPENASLYAELASfqnkqnklwqsvdswgeaisrdsvhaewfyqygiVLEKLGHFLQASKAYEQAks 215
Cdd:COG2956   25 DKAIDLLEEALELDPETVEAHLALGN----------------------------------LYRRRGEYDRAIRIHQKL-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  216 LSMKENLSDLYFRLGFVNENQGHDNEidlevAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNN 295
Cdd:COG2956   69 LERDPDRAEALLELAQDYLKAGLLDR-----AEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPEN 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  296 PELLYRLGFAYDRNYQFGQAENIYKEALSL-KQKPEWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYwFYRSAYTL 374
Cdd:COG2956  144 AHAYCELAELYLEQGDYDEAIEALEKALKLdPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPA-LPRLAELY 222

                        250
                 ....*....|....*.
gi 34147958  375 EKQGLYEKASKMYLKL 390
Cdd:COG2956  223 EKLGDPEEALELLRKA 238
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 266-392 2.82e-13

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 68.29  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  266 FGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQK-PEWRFRLGFVQERQNK 344
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDePEARLNLGLALLKAGD 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 34147958  345 FDQATINYEQAATERKQYtPYWFYRSAYTLEKQGLYEKASKMYLKLRK 392
Cdd:COG4783   88 YDEALALLEKALKLDPEH-PEAYLRLARAYRALGRPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 166-392 5.50e-13

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.49  E-value: 5.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  166 QNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGHDNEI--- 242
Cdd:COG3914   14 AAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLA--LAAGEAAAAAAALLLLAALLELAALLLqal 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 -DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKE 321
Cdd:COG3914   92 gRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34147958  322 ALSLK-QKPEWRFRLGFVQERQNKFDQATINYEQAATERKQYtPYWFYRSAYTLEKQGLYEKASKMYLKLRK 392
Cdd:COG3914  172 ALELDpDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDN-ADAHSNLLFALRQACDWEVYDRFEELLAA 242
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 1144-1246 3.47e-12

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 69.69  E-value: 3.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1144 INSFANVVKKYPKTqLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILPSNHEGQPMTLFEAMILE 1223
Cdd:cd04962  215 VRVFARVRRKIPAK-LLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACG 293

                         90       100
                 ....*....|....*....|....
gi 34147958 1224 KMIIATDIVGSRSAL-EGRSGYLV 1246
Cdd:cd04962  294 VPVVSSNAGGIPEVVkHGETGFLS 317
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1178-1262 3.49e-12

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 64.63  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1178 LGLEKNVHLLgLRAnpfpLLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLVE-NSVSGLEK 1255
Cdd:COG0438    4 LVPRKGLDLL-LEA----LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdGETGLLVPpGDPEALAE 78


                 ....*..
gi 34147958 1256 GMLDYIS 1262
Cdd:COG0438   79 AILRLLE 85
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 280-412 3.89e-12

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 64.64  E-value: 3.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  280 RAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQATINYEQAATE 358
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDpDNADALLDLAEALLAAGDTEEAEELLERALAL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34147958  359 RKQYTPYWFYRsAYTLEKQGLYEKASKMYLKLrknteLALKNKIHNKEAVEKLI 412
Cdd:COG4235   81 DPDNPEALYLL-GLAAFQQGDYAEAIAAWQKL-----LALLPADAPARLLEASI 128
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 18-480 5.23e-12

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 70.50  E-value: 5.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEILQwqvqlrqsevrirl 97
Cdd:TIGR02917  265 YLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQ-------------- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     98 kkhkkksvigktsvhkiveeqqkinideIKRItsssandiaeqiiidalekepenaslyaeLASFQNKQNKLWQSVDSWG 177
Cdd:TIGR02917  331 ----------------------------ARRL-----------------------------LASIQLRLGRVDEAIATLS 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLsmKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQA 257
Cdd:TIGR02917  354 PALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATEL--DPENAAARTQLGISKLSQG-----DPSEAIADLETAAQL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    258 DRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQK-PEWRFRLG 336
Cdd:TIGR02917  427 DPELGRADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDfFPAAANLA 506

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    337 FVQERQNKFDQATINYEQAATERKQYTPY------WFYRSAYTLEKQGLYEKASKmylklRKNTELALK-----NKIHNK 405
Cdd:TIGR02917  507 RIDIQEGNPDDAIQRFEKVLTIDPKNLRAilalagLYLRTGNEEEAVAWLEKAAE-----LNPQEIEPAlalaqYYLGKG 581

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147958    406 EAvEKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAeLAYYQAVSRSEILNSLGYYRLAFVQLKQNKYEEA 480
Cdd:TIGR02917  582 QL-KKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKA-VSSFKKLLALQPDSALALLLLADAYAVMKNYAKA 654
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 134-330 2.28e-11

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.10  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  134 ANDIAEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQA 213
Cdd:COG3914   59 LLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  214 ksLSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITP 293
Cdd:COG3914  139 --LALNPDFAEAYLNLGEALRRLG-----RLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDP 211

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 34147958  294 NNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQKPE 330
Cdd:COG3914  212 DNADAHSNLLFALRQACDWEVYDRFEELLAALARGPS 248
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
145-362 8.55e-11

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.87  E-value: 8.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  145 ALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSD 224
Cdd:COG0457   34 ALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKA--LELDPDDAE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  225 LYFRLGFVNENQGhdneiDLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGF 304
Cdd:COG0457  112 ALYNLGLALLELG-----RYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEA 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34147958  305 AYDRNYQFGQAENIYKEALSLKQKPEWRFRLGFVQERQNKFDQATINYEQAATERKQY 362
Cdd:COG0457  187 ALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYR 244
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 187-328 1.10e-10

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 60.98  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  187 AEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGHDNEidlevAKQAYGLAIQADRKLRAKDF 266
Cdd:COG4783    4 AEALYALAQALLLAGDYDEAEALLEKA--LELDPDNPEAFALLGEILLQLGDLDE-----AIVLLHEALELDPDEPEARL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34147958  267 GIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQK 328
Cdd:COG4783   77 NLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 26-474 1.70e-10

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 65.49  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     26 QKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEILQWQVQLRQSevriRLKKHKKKSV 105
Cdd:TIGR02917  375 ALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLLLILS----YLRSGQFDKA 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    106 IgktSVHKIVEEQQKIN--IDEIKRITSSSANDI--AEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAIS 181
Cdd:TIGR02917  451 L---AAAKKLEKKQPDNasLHNLLGAIYLGKGDLakAREAFEKALSIEPDFFPAAANLARIDIQEGNPDDAIQRFEKVLT 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    182 RDSVHAEWFYQYGIVLEKLGHFLQASKAYEQA-----KSLSMKENLSDLYFRLGFVNENQGHDNEIDLEVAKQAYGLAIQ 256
Cdd:TIGR02917  528 IDPKNLRAILALAGLYLRTGNEEEAVAWLEKAaelnpQEIEPALALAQYYLGKGQLKKALAILNEAADAAPDSPEAWLML 607

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    257 ADRKLRAKDFGIGV----------------------FHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQ 314
Cdd:TIGR02917  608 GRAQLAAGDLNKAVssfkkllalqpdsalalllladAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTES 687

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    315 AENIYKEAlsLKQKPEWRFR---LGFVQERQNKFDQATINYEQAaterkqytpYWFYRSAYTLEKQGLYEKASKmylklr 391
Cdd:TIGR02917  688 AKKIAKSL--QKQHPKAALGfelEGDLYLRQKDYPAAIQAYRKA---------LKRAPSSQNAIKLHRALLASG------ 750

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    392 kntelalknkiHNKEAVEKLIFILNKkhqyDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRSE----ILNSlgyyrL 467
Cdd:TIGR02917  751 -----------NTAEAVKTLEAWLKT----HPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPdnavVLNN-----L 810


                   ....*..
gi 34147958    468 AFVQLKQ 474
Cdd:TIGR02917  811 AWLYLEL 817
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 1126-1253 2.39e-10

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 63.93  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1126 KVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPL-VQQIKQLGLEKNVHLLGlranPFP------LLK 1198
Cdd:cd03821  205 RIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPAfLQLQSSLGLGDRVTFTG----PLYgeakwaLYA 280

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 34147958 1199 KADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALEGRSGYLVENSVSGL 1253
Cdd:cd03821  281 SADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDPNVSSL 335
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 243-355 2.91e-10

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 59.97  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEA 322
Cdd:COG5010   35 NNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKA 114

                         90       100       110
                 ....*....|....*....|....*....|....
gi 34147958  323 LSLKQK-PEWRFRLGFVQERQNKFDQATINYEQA 355
Cdd:COG5010  115 LALSPDnPNAYSNLAALLLSLGQDDEAKAALQRA 148
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
18-288 3.82e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.95  E-value: 3.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEilQWQVQLRQSEVRIRL 97
Cdd:COG0457   12 NNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD--DAEALNNLGLALQAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   98 KKHKKksvigktsvhkiveeqqkinideikritsssandiAEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWG 177
Cdd:COG0457   90 GRYEE-----------------------------------ALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLSMKENLSDLYFRLGFVNENQGHDNEIDLEVAKQAYGLAIQA 257
Cdd:COG0457  135 RALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAIL 214

                        250       260       270
                 ....*....|....*....|....*....|.
gi 34147958  258 DRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQ 288
Cdd:COG0457  215 TLAALAELLLLALALLLALRLAALALYQYRA 245
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 1131-1240 7.43e-10

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 63.12  E-value: 7.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1131 IGRLSIEKDHAKLINSFANVVKKYPKTQLLIIG--DGSLRYplVQQ----IKQLGLEKNVHLLGlRANPFPLLKKADCFI 1204
Cdd:cd03813  299 VGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGpeDEDPEY--AQEckrlVASLGLENKVKFLG-FQNIKEYYPKLGLLV 375

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 34147958 1205 LPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALEG 1240
Cdd:cd03813  376 LTSISEGQPLVILEAMASGVPVVATDVGSCRELIYG 411
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 1126-1249 7.46e-10

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 62.29  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1126 KVFLTIGRLSIEKDHAKLINsfANVVKKYPktqLLIIGDGSLRYPLVQQIKqLGLEKNVHLLGLRANP--FPLLKKADCF 1203
Cdd:cd03795  192 KIFLFIGRLVYYKGLDYLIE--AAQYLNYP---IVIGGEGPLKPDLEAQIE-LNLLDNVKFLGRVDDEekVIYLHLCDVF 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 34147958 1204 ILPS--NHEGQPMTLFEAMILEKMIIATDIVGSRS--ALEGRSGYLVENS 1249
Cdd:cd03795  266 VFPSvlRSEAFGIVLLEAMMCGKPVISTNIGTGVPyvNNNGETGLVVPPK 315
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 138-258 8.72e-10

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 58.28  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  138 AEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLS 217
Cdd:COG4783   23 AEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKA--LK 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 34147958  218 MKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQAD 258
Cdd:COG4783  101 LDPEHPEAYLRLARAYRALG-----RPDEAIAALEKALELD 136
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 277-355 9.04e-10

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 58.09  E-value: 9.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  277 DWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQATINYEQA 355
Cdd:COG4235   32 RYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDpDNPEALYLLGLAAFQQGDYAEAIAAWQKL 111
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 202-453 1.26e-09

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 62.70  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  202 HFLQASKAYEQAKSLSMKENLSDLYFRLGFVNENQGHDNEIDLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRA 281
Cdd:COG3914   18 LAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  282 IIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQK-PEWRFRLGFVQERQNKFDQATINYEQAAterk 360
Cdd:COG3914   98 LALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDfAEAYLNLGEALRRLGRLEEAIAALRRAL---- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  361 qytpywfyrsaytlekqglyekaskmylklrkntelalknkihnkeaveklifilnkkhQYDASSAESWFDLGTYYEFLN 440
Cdd:COG3914  174 -----------------------------------------------------------ELDPDNAEALNNLGNALQDLG 194

                        250
                 ....*....|...
gi 34147958  441 DWEQAELAYYQAV 453
Cdd:COG3914  195 RLEEAIAAYRRAL 207
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 116-258 1.47e-09

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 62.32  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  116 EEQQKINIDEIKRITSSSANDIAEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGI 195
Cdd:COG3914   75 LLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGE 154

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34147958  196 VLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQAD 258
Cdd:COG3914  155 ALRRLGRLEEAIAALRRA--LELDPDNAEALNNLGNALQDLG-----RLEEAIAAYRRALELD 210
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 1065-1280 5.26e-09

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 59.65  E-value: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1065 DKVISVSELTMKLnqdklsdrfniplskfdYSDNLQQPEKIKV--------LARDElleqdKAYFNTEDKVFLTIGRLSI 1136
Cdd:cd03823  145 DAVLAPSRFTANL-----------------HEANGLFSARISVipnavepdLAPPP-----RRRPGTERLRFGYIGRLTE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1137 EKDHAKLINSFANVvkKYPKTQLLIIGDGSLryplvQQIKQLGLEKNVHLLGL--RANPFPLLKKADCFILPSN-HEGQP 1213
Cdd:cd03823  203 EKGIDLLVEAFKRL--PREDIELVIAGHGPL-----SDERQIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIwPEPFG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147958 1214 MTLFEAMILEKMIIATDIVGSRSAL-EGRSGYLVE-NSVSGLEKGMLDYISGSLPLVTYDINEYQKQAI 1280
Cdd:cd03823  276 LVVREAIAAGLPVIASDLGGIAELIqPGVNGLLFApGDAEDLAAAMRRLLTDPALLERLRAGAEPPRST 344
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
1130-1249 8.87e-09

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 59.71  E-value: 8.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  1130 TIG---RLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKKADCFILP 1206
Cdd:PRK15490  400 TIGgvfRFVGDKNPFAWIDFAARYLQHHPATRFVLVGDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILF 479

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 34147958  1207 SNHEGQPMTLFEAMILEKMIIATDIVGSRSA-LEGRSGYLVENS 1249
Cdd:PRK15490  480 SRYEGLPNVLIEAQMVGVPVISTPAGGSAECfIEGVSGFILDDA 523
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
272-355 2.56e-08

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 52.87  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  272 HEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENiYKEALSLK-QKPEWRFRLGFVQERQNKFDQATI 350
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDpNNAEALLNLAELLLELGDYDEALA 80


                 ....*
gi 34147958  351 NYEQA 355
Cdd:COG3063   81 YLERA 85
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 40-485 2.64e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 58.56  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     40 AVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEilqwQVQLRQSEVRIRLKKHKKKSVIGKTSVHKIVEEQQ 119
Cdd:TIGR02917   48 ALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYP----KNQVLPLLARAYLLQGKFQQVLDELPGKTLLDDEG 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    120 KINIDEIKRITS--SSANDIAEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVL 197
Cdd:TIGR02917  124 AAELLALRGLAYlgLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADPGNVDALLLKGDLL 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    198 EKLGHFLQASKAYEQAKSLSmKENLSDLYFRLGfVNENQGHDNEIDlevaKQAYGLAIQADRKLRAKdFGIGVFHEHRRD 277
Cdd:TIGR02917  204 LSLGNIELALAAYRKAIALR-PNNIAVLLALAT-ILIEAGEFEEAE----KHADALLKKAPNSPLAH-YLKALVDFQKKN 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    278 WGRAIIAYKAQLEITPNNPELLYRLGFAYdrnYQFGQAENIYkEALS--LKQKPEW---RFRLGFVQERQNKFDQAtINY 352
Cdd:TIGR02917  277 YEDARETLQDALKSAPEYLPALLLAGASE---YQLGNLEQAY-QYLNqiLKYAPNShqaRRLLASIQLRLGRVDEA-IAT 351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    353 EQAATERKQYTPYWFYRSAYTLEKQGLYEKASKMylkLRKNTELALKNKIHN-KEAVEKLIfilnkkhQYDASSAESwfD 431
Cdd:TIGR02917  352 LSPALGLDPDDPAALSLLGEAYLALGDFEKAAEY---LAKATELDPENAAARtQLGISKLS-------QGDPSEAIA--D 419

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    432 LGTYYEFLNDWEQAELA----YYQ------AVSRSEIL------NSLGYYRLAFVQLKQNKYEEACENFR 485
Cdd:TIGR02917  420 LETAAQLDPELGRADLLlilsYLRsgqfdkALAAAKKLekkqpdNASLHNLLGAIYLGKGDLAKAREAFE 489
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
200-409 3.77e-08

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 55.31  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  200 LGHFLQASKAYEQAKSLSMKENLSDLYFRLGFVNENQGHDNEIDLEVAKQAYGLAIQADRKLRAKD-FGIGVFHEHRRDW 278
Cdd:COG4785   10 LALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLyYERGVAYDSLGDY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  279 GRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQATINYEQAAT 357
Cdd:COG4785   90 DLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDpDYAYAYLNRGIALYYLGRYELAIADLEKALE 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34147958  358 ERKQ--YTPYWFYRSAYTLEKQGLYEKASKMYLKLRKNTELALKNKIHNKEAVE 409
Cdd:COG4785  170 LDPNdpERALWLYLAERKLDPEKALALLLEDWATAYLLQGDTEEARELFKLALA 223
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 332-485 5.33e-08

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 55.89  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  332 RFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKASKMYLKLRKNTElalknkiHNKEAVEKL 411
Cdd:COG2956   11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLAL-GNLYRRRGEYDRAIRIHQKLLERDP-------DRAEALLEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  412 IFILNKKHQYD-------------ASSAESWFDLGTYYEFLNDWEQAeLAYYQAVSRSEILNSLGYYRLAFVQLKQNKYE 478
Cdd:COG2956   83 AQDYLKAGLLDraeelleklleldPDDAEALRLLAEIYEQEGDWEKA-IEVLERLLKLGPENAHAYCELAELYLEQGDYD 161


                 ....*..
gi 34147958  479 EACENFR 485
Cdd:COG2956  162 EAIEALE 168
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 54-476 5.57e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 57.40  E-value: 5.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958     54 LGMCFFKQGVWDKAYHYISIATNLAPEILQWQVQLRQSevriRLKKHKKKSVIGktSVHKIVE-EQQKIN------IDEI 126
Cdd:TIGR02917  369 LGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGIS----KLSQGDPSEAIA--DLETAAQlDPELGRadllliLSYL 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    127 KRITSSSANDIAEQIiidaLEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHA-EWFYQYGIVLEKlGHFLQ 205
Cdd:TIGR02917  443 RSGQFDKALAAAKKL----EKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFpAAANLARIDIQE-GNPDD 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    206 ASKAYEQA-----KSLSMKENLSDLYFRLGfvnenqghdneiDLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGR 280
Cdd:TIGR02917  518 AIQRFEKVltidpKNLRAILALAGLYLRTG------------NEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKK 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    281 AIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSLK-QKPEWRFRLGFVQERQNkfdqatiNYEQAATEr 359
Cdd:TIGR02917  586 ALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQpDSALALLLLADAYAVMK-------NYAKAITS- 657

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    360 kqytpywfYRSAYTLEKqGLYEkaskmyLKLRKNTELALKNKIhnkEAVEKLIFILNKKHQYDASSAESwfdLGTYYEFL 439
Cdd:TIGR02917  658 --------LKRALELKP-DNTE------AQIGLAQLLLAAKRT---ESAKKIAKSLQKQHPKAALGFEL---EGDLYLRQ 716

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 34147958    440 NDWEQAELAYYQAVSRSEILNSLGYYRLAFVQLKQNK 476
Cdd:TIGR02917  717 KDYPAAIQAYRKALKRAPSSQNAIKLHRALLASGNTA 753
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 1030-1262 5.92e-08

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 56.58  E-value: 5.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1030 IKNKKSSIYMH----NSMEEEYRLKYPYLKSIF-----YYCSLADKVISVSELtmklNQDKLSDRFnIPLSKFDYSDNLQ 1100
Cdd:cd03794  121 LRGAPFILDVRdlwpESLIALGVLKKGSLLKLLkklerKLYRLADAIIVLSPG----LKEYLLRKG-VPKEKIIVIPNWA 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1101 QPEKIKVLARDELleqdKAYFNTEDK-VFLTIGRLSIEKDHAKLINSfANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLG 1179
Cdd:cd03794  196 DLEEFKPPPKDEL----RKKLGLDDKfVVVYAGNIGKAQGLETLLEA-AERLKRRPDIRFLFVGDGDEKERLKELAKARG 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1180 LEkNVHLLGL--RANPFPLLKKADCFILP-----SNHEGQPMTLFEAMILEKMIIATDIVGSRSA-LEGRSGYLVEN-SV 1250
Cdd:cd03794  271 LD-NVTFLGRvpKEEVPELLSAADVGLVPlkdnpANRGSSPSKLFEYMAAGKPILASDDGGSDLAvEINGCGLVVEPgDP 349

                        250
                 ....*....|..
gi 34147958 1251 SGLEKGMLDYIS 1262
Cdd:cd03794  350 EALADAILELLD 361
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 1124-1246 8.11e-08

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 55.92  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1124 EDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGlekNVHLLGL--RANPFPLLKKAD 1201
Cdd:cd05844  188 RAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALG---RVRFLGAlpHAEVQDWMRRAE 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34147958 1202 CFILPS------NHEGQPMTLFEAMILEKMIIATDIVGSRSA-LEGRSGYLV 1246
Cdd:cd05844  265 IFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAiLDGETGFLV 316
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 330-485 8.66e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.50  E-value: 8.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  330 EWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKASKMYlklrkntelalknkihnKEAVE 409
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALL-GEILLQLGDLDEAIVLL-----------------HEALE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34147958  410 KlifilnkkhqyDASSAESWFDLGTYYEFLNDWEQAeLAYYQAVSRSEILNSLGYYRLAFVQLKQNKYEEACENFR 485
Cdd:COG4783   67 L-----------DPDEPEARLNLGLALLKAGDYDEA-LALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALE 130
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 147-480 1.58e-07

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 55.86  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    147 EKEPEnaSLYAELASFQNKqNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLSMKENLSDLY 226
Cdd:TIGR02917   19 DQSPE--ELIEAAKSYLQK-NKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYPKNQVLPL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    227 frLGFVNENQGHDNEIdLEVAKQAYGLaiqaDRKLRAKDFGI-GVFHEHRRDWGRAIIAYKAQLEITPNNPELlyRLGFA 305
Cdd:TIGR02917   96 --LARAYLLQGKFQQV-LDELPGKTLL----DDEGAAELLALrGLAYLGLGQLELAQKSYEQALAIDPRSLYA--KLGLA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    306 YDR--NYQFGQAENIYKEALSL--KQKPEWRFRlGFVQERQNKFDQATINYEQAATERKQYTPYWFYRsAYTLEKQGLYE 381
Cdd:TIGR02917  167 QLAlaENRFDEARALIDEVLTAdpGNVDALLLK-GDLLLSLGNIELALAAYRKAIALRPNNIAVLLAL-ATILIEAGEFE 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    382 KASKMYLKLRK---NTELA--LKNKIHNKE-----AVEKLIFILnkkhQYDASSAESWFDLGTYYEFLNDWEQAELAYYQ 451
Cdd:TIGR02917  245 EAEKHADALLKkapNSPLAhyLKALVDFQKknyedARETLQDAL----KSAPEYLPALLLAGASEYQLGNLEQAYQYLNQ 320

                          330       340       350
                   ....*....|....*....|....*....|
gi 34147958    452 AVSRSEilNSLGYYR-LAFVQLKQNKYEEA 480
Cdd:TIGR02917  321 ILKYAP--NSHQARRlLASIQLRLGRVDEA 348
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 178-325 1.77e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.55  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  178 EAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneidlevakqayglaiqa 257
Cdd:COG4235    8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKA--LRLDPDNADALLDLAEALLAAG-------------------- 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34147958  258 drklrakdfgigvfhehrrDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEALSL 325
Cdd:COG4235   66 -------------------DTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 138-338 3.75e-07

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 54.61  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  138 AEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLS 217
Cdd:COG3914  131 ALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRA--LE 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  218 MKENLSDLYFRLGFVNENQGHDNEIDLEVAKQAYglaiqadrkLRAKDFGIGVFHEHRrdwgraiiaykaqleITPNNPE 297
Cdd:COG3914  209 LDPDNADAHSNLLFALRQACDWEVYDRFEELLAA---------LARGPSELSPFALLY---------------LPDDDPA 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 34147958  298 LLYRLGFAYDRNYQFGQAENIykEALSLKQKPEWRFRLGFV 338
Cdd:COG3914  265 ELLALARAWAQLVAAAAAPEL--PPPPNPRDPDRKLRIGYV 303
MamA NF040959
magnetosome protein MamA; Magnetosomes are special lipid-bound organelles that comprise ...
 153-348 4.98e-07

magnetosome protein MamA; Magnetosomes are special lipid-bound organelles that comprise magnetic mineral crystals in magnetotactic bacteria (MTB). Magnetosomes are important for MTB to search for preferred microaerophilic environment. Proteins of this family typically contain five tetra-trico-peptide repeat (TPR) motifs. Based on structural analyses, MamA forms a large homooligomer through self-recognition to regulate protein-protein interaction in magnetosomes.


Pssm-ID: 468889 [Multi-domain]  Cd Length: 204  Bit Score: 51.61  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   153 ASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLsmkenlsdlyfrlgfv 232
Cdd:NF040959   37 AKMYRNKGISHAKKGRYDKAVRYLEQVARIDPDDVEALYRLGVAYLKTGQYDRAIKVLEKVLSL---------------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   233 nenqGHDNeidlevAKQAYGLAIQAdrkLRAKDFGigvfhehrrdwgRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQF 312
Cdd:NF040959  101 ----APDH------VKAAYRKGVAL---LKIKDYE------------KAVEDLEEALEEKPDNFNLNYRLGLALDGLGQY 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 34147958   313 GQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQA 348
Cdd:NF040959  156 DKAIEAFQKALELDpNEIKYHQAIGFMYVQKGDHETA 192
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 1118-1262 5.06e-07

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 53.54  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1118 KAYFNTEDK-VFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIG-------DGSLRYPLVQQIKQLGLEKNV--HLL 1187
Cdd:cd03822  179 KRLLLPEGKkVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelhpslaRYEGERYRKAAIEELGLQDHVdfHNN 258

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147958 1188 GLRANPFP-LLKKADCFILP--SNHEGQPMTLFEAMILEKMIIATDIVGSRSALEGRSGYLVE-NSVSGLEKGMLDYIS 1262
Cdd:cd03822  259 FLPEEEVPrYISAADVVVLPylNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRGVLVPfDDPSAIAEAILRLLE 337
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
1122-1285 8.05e-07

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 52.79  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  1122 NTEDKVFLTIGRLSIE--KDHAKLINSFANVVKKYpktQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLL-- 1197
Cdd:PRK09922  177 RDKPAVFLYVGRLKFEgqKNVKELFDGLSQTTGEW---QLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVqq 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  1198 --KKADCFILPSNHEGQPMTLFEAMILEKMIIATDIV-GSRSAL-EGRSGYLVE-NSVSGLEKGMLDYISGSLPLVTYDI 1272
Cdd:PRK09922  254 kiKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMsGPRDIIkPGLNGELYTpGNIDEFVGKLNKVISGEVKYQHDAI 333

                         170
                  ....*....|...
gi 34147958  1273 neyqKQAINKFYS 1285
Cdd:PRK09922  334 ----PNSIERFYE 342
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 293-356 8.58e-07

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 52.61  E-value: 8.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34147958  293 PNNPELLYRLGFAYDRNYQFGQAENIYKEALSLKQKPEWRFRLGFVQERQNKFDQATINYEQAA 356
Cdd:COG3071  255 PNDPDLLLALGRLCLRNQLWGKAREYLEAALALRPSAEAYAELARLLEQLGDPEEAAEHYRKAL 318
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 243-397 1.05e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 49.96  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIIAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEA 322
Cdd:COG5010    1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34147958  323 LSLK-QKPEWRFRLGFVQERQNKFDQATINYEQAAtERKQYTPYWFYRSAYTLEKQGLYEKASKMYLKLRKNTELA 397
Cdd:COG5010   81 LQLDpNNPELYYNLALLYSRSGDKDEAKEYYEKAL-ALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPLK 155
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
134-324 1.99e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 50.30  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  134 ANDIAEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQA 213
Cdd:COG4785   54 AAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  214 ksLSMKENLSDLYFRLGFVNENQGhdneiDLEVAKQAYGLAIQADRKlrakdfgigvfhehrrDWGRAIIAYKAQLEITP 293
Cdd:COG4785  134 --LELDPDYAYAYLNRGIALYYLG-----RYELAIADLEKALELDPN----------------DPERALWLYLAERKLDP 190

                        170       180       190
                 ....*....|....*....|....*....|...
gi 34147958  294 NNP--ELLYRLGFAYDRNYQFGQAENIYKEALS 324
Cdd:COG4785  191 EKAlaLLLEDWATAYLLQGDTEEARELFKLALA 223
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 1080-1246 3.02e-06

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 51.17  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1080 DKLSDrFNIPLSKFDYSDNLQQPEKIkvlardelleqdkayfNTEDKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQL 1159
Cdd:cd03792  169 DPLSG-KNKDLSPADIRYYLEKPFVI----------------DPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQL 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1160 LIIG-------DGSLRYPLVQQIKqlGLEKNVHLLglRANPF-----PLLKKADCFILPSNHEGQPMTLFEAMILEKMII 1227
Cdd:cd03792  232 VICGhgavddpEGSVVYEEVMEYA--GDDHDIHVL--RLPPSdqeinALQRAATVVLQLSTREGFGLTVSEALWKGKPVI 307

                        170       180
                 ....*....|....*....|
gi 34147958 1228 ATDIVGSRSALE-GRSGYLV 1246
Cdd:cd03792  308 ATPAGGIPLQVIdGETGFLV 327
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 144-265 3.87e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 47.69  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  144 DALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLS 223
Cdd:COG4235    8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERA--LALDPDNP 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 34147958  224 DLYFRLGFVNENQGHdneidlevakqaYGLAIQADRKLRAKD 265
Cdd:COG4235   86 EALYLLGLAAFQQGD------------YAEAIAAWQKLLALL 115
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 18-67 1.12e-05

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 45.75  E-value: 1.12e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 34147958   18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAY---SNFKLGMCFFKQGVWDKA 67
Cdd:COG1729   34 YWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGDYDKA 86
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 351-485 1.93e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.84  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  351 NYEQAATERKQYTPYWFYRSAYTLEKQGLYEKASKMYLKLRKNTELALKNKIHNKEAVEKLIFILNKKHQYDA------- 423
Cdd:COG3914   24 AELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEalalyrr 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34147958  424 ------SSAESWFDLGTYYEFLNDWEQAELAYYQAVsRSEILNSLGYYRLAFVQLKQNKYEEACENFR 485
Cdd:COG3914  104 alalnpDNAEALFNLGNLLLALGRLEEALAALRRAL-ALNPDFAEAYLNLGEALRRLGRLEEAIAALR 170
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 138-217 3.32e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.00  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  138 AEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLS 217
Cdd:COG4235   36 ALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALL 115
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 1123-1253 3.58e-05

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 48.11  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  1123 TEDKVFlTIG---RLSIEKDHAKLINSFANVVKKYPKTQLLIIGDGSLRYPLVQQIKQLGLEKNVHLLGLRANPFPLLKK 1199
Cdd:PRK15179  513 TSDARF-TVGtvmRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSRRVGYWLTQ 591

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 34147958  1200 ADCFILPSNHEGQPMTLFEAMILEKMIIATdivgsrsaLEGRSGYLVENSVSGL 1253
Cdd:PRK15179  592 FNAFLLLSRFEGLPNVLIEAQFSGVPVVTT--------LAGGAGEAVQEGVTGL 637
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
243-326 3.75e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 43.62  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  243 DLEVAKQAYGLAIQADRKLRAKDFGIGVFHEHRRDWGRAIiAYKAQLEITPNNPELLYRLGFAYDRNYQFGQAENIYKEA 322
Cdd:COG3063    7 DLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERA 85


                 ....
gi 34147958  323 LSLK 326
Cdd:COG3063   86 LELD 89
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
305-399 3.94e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 43.62  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  305 AYDRNYQFGQAENIYKEALSLK-QKPEWRFRLGFVQERQNKFDQAtINYEQAATERKQYTPYWFYRsAYTLEKQGLYEKA 383
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDpDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNL-AELLLELGDYDEA 78

                         90
                 ....*....|....*.
gi 34147958  384 SKMYLKLRKNTELALK 399
Cdd:COG3063   79 LAYLERALELDPSALR 94
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 1113-1246 6.45e-05

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 46.85  E-value: 6.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1113 LLEQDKayfntedKVFLTIGRLSIEKDHAKLINSFANVVKKYPKTQLLIIG-----DGSLRYPLVQQI-KQLGLEKNVHL 1186
Cdd:cd03800  215 LLPPDK-------PVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGgpsddPLSMDREELAELaEELGLIDRVRF 287

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34147958 1187 LG-LRANPFP-LLKKADCFILPSNHEGQPMTLFEAMILEKMIIATDIVGSRSALE-GRSGYLV 1246
Cdd:cd03800  288 PGrVSRDDLPeLYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRdGRTGLLV 350
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 304-393 6.55e-05

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 43.44  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  304 FAYDRNYQFGQAENIYKEALSL----KQKPEWRFRLGFVQERQNKFDQATINYEQAATERKQ--YTPYWFYRSAYTLEKQ 377
Cdd:COG1729    1 KALLKAGDYDEAIAAFKAFLKRypnsPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDspKAPDALLKLGLSYLEL 80

                         90
                 ....*....|....*.
gi 34147958  378 GLYEKASKMYLKLRKN 393
Cdd:COG1729   81 GDYDKARATLEELIKK 96
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 1110-1247 7.65e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 46.52  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958 1110 RDELLEQDKAyfntedkVFLTIGRLSIEKDHAKLINSFANVVKKYPkTQLLIIGDGSLRYPLvqQIKQLglekNVHLLGL 1189
Cdd:cd03814  190 RRRLGPPGRP-------LLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGDGPARAEL--EARGP----DVIFTGF 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147958 1190 R-----ANpfpLLKKADCFILPSNHEgqpmTlFEAMILEKM-----IIATDIVGSRSAL-EGRSGYLVE 1247
Cdd:cd03814  256 LtgeelAR---AYASADVFVFPSRTE----T-FGLVVLEAMasglpVVAADAGGPRDIVrPGGTGALVE 316
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 13-102 1.24e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 43.26  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   13 NTPVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEilQWQVQLRQSE 92
Cdd:COG4783   37 NPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPE--HPEAYLRLAR 114

                         90
                 ....*....|
gi 34147958   93 VRIRLKKHKK 102
Cdd:COG4783  115 AYRALGRPDE 124
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
138-217 1.36e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.08  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  138 AEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDsWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLS 217
Cdd:COG3063   11 AEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELD 89
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 18-67 1.82e-04

tol-pal system protein YbgF; Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction.


Pssm-ID: 188247 [Multi-domain]  Cd Length: 117  Bit Score: 42.27  E-value: 1.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 34147958     18 YWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSN---FKLGMCFFKQGVWDKA 67
Cdd:TIGR02795   41 YWLGEAYYAQGDYADAAKAFLAVVKKYPKSPKAPdalLKLGMSLQELGDKEKA 93
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 138-217 1.94e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 43.41  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  138 AEQIIIDALEKEPENASLYAELASFQNKQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLS 217
Cdd:COG5010   73 SLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTS 152
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 410-485 3.15e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 3.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34147958  410 KLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRSEiLNSLGYYRLAFVQLKQNKYEEACENFR 485
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDP-DNADALLDLAEALLAAGDTEEAEELLE 75
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 13-216 3.33e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.95  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   13 NTPVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPEILqwQVQLRQSE 92
Cdd:COG2956  109 DAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCA--RALLLLAE 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   93 VRIRLKKHKKksvigktsvhkiveeqqkinideikritsssandiAEQIIIDALEKEPENASLYAELASFQNKQNKLWQS 172
Cdd:COG2956  187 LYLEQGDYEE-----------------------------------AIAALERALEQDPDYLPALPRLAELYEKLGDPEEA 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 34147958  173 VDSWGEAISRDSVHAEWFYqygivlekLGHFLQASKAYEQAKSL 216
Cdd:COG2956  232 LELLRKALELDPSDDLLLA--------LADLLERKEGLEAALAL 267
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 15-217 4.50e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.72  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   15 PVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYhyisiatnlapeilqwqVQLRQsevr 94
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAI-----------------VLLHE---- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958   95 irlkkhkkksvigktsvhkiveeqqkinideikritsssandiaeqiiidALEKEPENASLYAELASFQNKQNKLWQSVD 174
Cdd:COG4783   64 --------------------------------------------------ALELDPDEPEARLNLGLALLKAGDYDEALA 93

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 34147958  175 SWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAKSLS 217
Cdd:COG4783   94 LLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 2-79 5.00e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.25  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    2 KKAFYKATRLL--NTPVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAP 79
Cdd:COG5010   74 LALLEQALQLDpnNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
Ycf37 COG5714
Photosystem I assembly protein Ycf37, contains TPR repeats [Energy production and conversion]; ...
 247-355 6.99e-04

Photosystem I assembly protein Ycf37, contains TPR repeats [Energy production and conversion]; Photosystem I assembly protein Ycf37, contains TPR repeats is part of the Pathway/BioSystem: Photosystem I


Pssm-ID: 444424 [Multi-domain]  Cd Length: 176  Bit Score: 41.85  E-value: 6.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  247 AKQAYGLA-IQADRKLRAKdfGIGVFHEhrrdwgraiiAYKAQLEITPNNPELLYR-LGFAYDRNYQFGQAENIYKEAls 324
Cdd:COG5714   52 AQEYYELGsIYLDKKLYVQ--AIALFQK----------ALKAAEEEEPENLALIYNaLGFAYFAQEQYDLAIRQYKEA-- 117

                         90       100       110
                 ....*....|....*....|....*....|....
gi 34147958  325 LKQKPEWRF---RLGFVQERQNKFDQATINYEQA 355
Cdd:COG5714  118 LKLKPDYVTalnNLGHAYEKKKLTAQALETYEEA 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 3-80 8.00e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 40.76  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    3 KAFYKATRLL--NTPVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPE 80
Cdd:COG4235   38 AAYEKALRLDpdNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPA 117
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
24-70 1.13e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.38  E-value: 1.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 34147958   24 FYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHY 70
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL 48
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
2-83 1.37e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.38  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    2 KKAFYKATRL--LNTPVIYWKGLHFYQKKDWEKAKYyFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAP 79
Cdd:COG3063   12 EEYYEKALELdpDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90


                 ....
gi 34147958   80 EILQ 83
Cdd:COG3063   91 SALR 94
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 24-80 1.78e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.33  E-value: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34147958   24 FYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPE 80
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPD 120
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 405-485 2.04e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 39.20  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  405 KEAVEKLIFILnKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSR--SEILNSLGYYRLAFVQLKQNKYEEACE 482
Cdd:COG1729   10 DEAIAAFKAFL-KRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRypDSPKAPDALLKLGLSYLELGDYDKARA 88


                 ...
gi 34147958  483 NFR 485
Cdd:COG1729   89 TLE 91
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 409-486 2.09e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.33  E-value: 2.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34147958  409 EKLIFILNKKHQYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRSEiLNSLGYYRLAFVQLKQNKYEEACENFRN 486
Cdd:COG5010   71 EESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSP-DNPNAYSNLAALLLSLGQDDEAKAALQR 147
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 165-258 3.07e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.94  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  165 KQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQASKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneiDL 244
Cdd:COG5010   66 KLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKA--LALSPDNPNAYSNLAALLLSLG-----QD 138

                         90
                 ....*....|....
gi 34147958  245 EVAKQAYGLAIQAD 258
Cdd:COG5010  139 DEAKAALQRALGTS 152
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 13-80 3.13e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 39.40  E-value: 3.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34147958   13 NTPVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPE 80
Cdd:COG4783   71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
165-263 4.39e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.84  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  165 KQNKLWQSVDSWGEAISRDSVHAEWFYQYGIVLEKLGHFLQAsKAYEQAksLSMKENLSDLYFRLGFVNENQGhdneiDL 244
Cdd:COG3063    4 KLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKA--LKLDPNNAEALLNLAELLLELG-----DY 75

                         90
                 ....*....|....*....
gi 34147958  245 EVAKQAYGLAIQADRKLRA 263
Cdd:COG3063   76 DEALAYLERALELDPSALR 94
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
320-482 4.52e-03

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 40.25  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  320 KEALSLKQKPEWRFRLGFVQERQNKFDQATINYEQAATERKQYTPYWFYRSAYTLEKQGLYEKAskmylklrkntelalk 399
Cdd:COG4700   80 EKALEFADTVQNRVRLADALLELGRYDEAIELYEEALTGIFADDPHILLGLAQALFELGRYAEA---------------- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958  400 nkihnKEAVEKLIfilNKKHQYDASSAEswFDLGTYYEFLNDWEQAELAYYQAVSRS---EilnslGYYRLAFVQLKQNK 476
Cdd:COG4700  144 -----LETLEKLI---AKNPDFKSSDAH--LLYARALEALGDLEAAEAELEALARRYsgpE-----ARYRYAKFLARQGR 208


                 ....*.
gi 34147958  477 YEEACE 482
Cdd:COG4700  209 TAEAKE 214
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 420-485 4.86e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.45  E-value: 4.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34147958  420 QYDASSAESWFDLGTYYEFLNDWEQAELAYYQAVSRsEILNSLGYYRLAFVQLKQNKYEEACENFR 485
Cdd:COG4235   45 RLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-DPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
3-97 8.59e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.60  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147958    3 KAFYKATRL--LNTPVIYWKGLHFYQKKDWEKAKYYFELAVQKKPEHAYSNFKLGMCFFKQGVWDKAYHYISIATNLAPE 80
Cdd:COG0457   97 EDYDKALELdpDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176

                         90
                 ....*....|....*..
gi 34147958   81 ILQWQVQLRQSEVRIRL 97
Cdd:COG0457  177 ALLAAALGEAALALAAA 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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