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Conserved domains on  [gi|696227561|ref|WP_032807848|]
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glucosaminidase domain-containing protein, partial [Oenococcus oeni]

Protein Classification

glycoside hydrolase family 73 protein( domain architecture ID 12811019)

glycoside hydrolase family 73 protein similar to Listeria monocytogenes virulence-associated peptidoglycan hydrolase Auto and Leuconostoc citreum atypical peptidoglycan hydrolase Mur

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 38-213 9.88e-53

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


:

Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 175.93  E-value: 9.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  38 ALVTTSSSTSSQAALEAEIEKIEAENTANYSSKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL-ASEYH 116
Cdd:COG1705   96 SANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSN 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 117 NLFGIKGSYN--GQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELLSENSRYSN-LIGETDAATAAEEIYEDGY 193
Cdd:COG1705  176 NLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGaLANAKDYEAFAKALQKAGY 255

                        170       180
                 ....*....|....*....|
gi 696227561 194 ATDPDYTEELEEIINEYNLT 213
Cdd:COG1705  256 ATDPKYADKLISIIESYNLT 275
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
71-361 9.62e-31

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 122.88  E-value: 9.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  71 VSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASE-YHNLFGIKGSYNGQTVDMPT-EEYYSGAYHEIDDY 148
Cdd:PRK06347 150 VQSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSApNYNLFGIKGAYNGQSYTKQTlEDDGKGNYYTITAK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 149 FRVYASDSESITDYEELL----SENSRYSNLI--GETDAATAAEEIYEDGYATDPDYTEELEEIINEYNLTAWDSlafky 222
Cdd:PRK06347 230 FRKYPSYHQSLEDYAQVIrkgpSWNPNYYSKVwkSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS----- 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 223 sGTVVTTTGSTSTSTSSTSSSSTSSSSKSYTVASGDTLTSIAKAYGTTVSAIATANNISNpDYIYVGEVLTIGSSTSTST 302
Cdd:PRK06347 305 -GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKS-DFIYPGQKLKVSAGSTTSD 382

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696227561 303 S---------TSSTSSSSTSSSSKSYTVASGDTLTSIAKAYGVSISTLAKLNNIsNTNLIYAGTTLKI 361
Cdd:PRK06347 383 TntskpstgtSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKV 449
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 38-213 9.88e-53

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 175.93  E-value: 9.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  38 ALVTTSSSTSSQAALEAEIEKIEAENTANYSSKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL-ASEYH 116
Cdd:COG1705   96 SANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSN 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 117 NLFGIKGSYN--GQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELLSENSRYSN-LIGETDAATAAEEIYEDGY 193
Cdd:COG1705  176 NLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGaLANAKDYEAFAKALQKAGY 255

                        170       180
                 ....*....|....*....|
gi 696227561 194 ATDPDYTEELEEIINEYNLT 213
Cdd:COG1705  256 ATDPKYADKLISIIESYNLT 275
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 74-216 3.97e-32

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 122.54  E-value: 3.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  74 FLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASEYHNLFGIK--GSYNGQTV---DMPTEEY-YSGAYHEIDD 147
Cdd:NF038016 163 FIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfGSPGPIAVgcrSYATFECsPTGGCFDTTA 242

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 148 YFRVYASDSESITDYEELLSENSRYSNLIGETDAATA-AEEIYEDGYATDPDYTEELEEIINEYNLTAWD 216
Cdd:NF038016 243 TFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQfAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
71-361 9.62e-31

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 122.88  E-value: 9.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  71 VSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASE-YHNLFGIKGSYNGQTVDMPT-EEYYSGAYHEIDDY 148
Cdd:PRK06347 150 VQSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSApNYNLFGIKGAYNGQSYTKQTlEDDGKGNYYTITAK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 149 FRVYASDSESITDYEELL----SENSRYSNLI--GETDAATAAEEIYEDGYATDPDYTEELEEIINEYNLTAWDSlafky 222
Cdd:PRK06347 230 FRKYPSYHQSLEDYAQVIrkgpSWNPNYYSKVwkSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS----- 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 223 sGTVVTTTGSTSTSTSSTSSSSTSSSSKSYTVASGDTLTSIAKAYGTTVSAIATANNISNpDYIYVGEVLTIGSSTSTST 302
Cdd:PRK06347 305 -GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKS-DFIYPGQKLKVSAGSTTSD 382

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696227561 303 S---------TSSTSSSSTSSSSKSYTVASGDTLTSIAKAYGVSISTLAKLNNIsNTNLIYAGTTLKI 361
Cdd:PRK06347 383 TntskpstgtSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKV 449
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 64-214 3.06e-28

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 107.52  E-value: 3.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561    64 TANYSSKVstFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASEYHNLFGIKGSYNGQTVDMPTEEYYSGAYH 143
Cdd:smart00047   3 LAGGSTLE--FVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGGWV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696227561   144 EIDDYFRVYASDSESITDYeELLSENSRYSNLIGETDAATAaeeiyedGYATDPDYTEELEEIINEYNLTA 214
Cdd:smart00047  81 TVKAAFRGYFGEKFIDYAY-VLRGQNPLYKKRWGSNALQTA-------GYATDPDYAKKLIRIIALYDEKL 143
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 74-209 5.02e-28

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 111.10  E-value: 5.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561   74 FLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL----ASEYHNLFGIK--GSYNGQTVDMPTEEYYSGAYHEIDD 147
Cdd:TIGR02541 151 FVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTA 230

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696227561  148 YFRVYASDSESITDYEELLSENSRYSNLIGETDAATAAEEIYEDGYATDPDYTEELEEIINE 209
Cdd:TIGR02541 231 KFRSYSSYEEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQS 292
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
93-207 2.04e-25

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 104.19  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  93 PSLTAAQAILESGWGTS----TLASEYHNLFGIK--GSYNGQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELL 166
Cdd:PRK05684 174 HHLLLAQAALESGWGQReirtADGSPSHNLFGIKadGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLL 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 696227561 167 SENSRYSNLIGETDAATAAEEIYEDGYATDPDYTEELEEII 207
Cdd:PRK05684 254 TNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVI 294
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 80-162 3.11e-22

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 89.55  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561   80 ESAINGWTQYKILPSLTAAQAILESGWGTSTLASEYHNLFGIKGSYNGQtVDMPTEEYYSGAyheiddYFRVYASDSESI 159
Cdd:pfam01832   2 PAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGK-VAYDTDEVTVAA------RFRKYDSVEESI 74


                  ...
gi 696227561  160 TDY 162
Cdd:pfam01832  75 RDY 77
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 250-294 1.13e-14

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 67.51  E-value: 1.13e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 696227561 250 KSYTVASGDTLTSIAKAYGTTVSAIATANNISNPDYIYVGEVLTI 294
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
178-361 1.19e-13

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 67.81  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 178 ETDAATAAEEIYEDGYATDPDYTEELEEIINEYNLTAWDSLAFKYSGTVVTTTGSTSTSTSSTSSSSTSSSSKSYTVASG 257
Cdd:COG1388   12 LLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 258 DTLTSIAKAYGTTVSAiatannisnpdyiyvgevltigsststststsstsssstssSSKSYTVASGDTLTSIAKAYGVS 337
Cdd:COG1388   92 DTLSGIARRYGAAAAP-----------------------------------------SPVTYTVKKGDTLWSIARRYGVS 130

                        170       180
                 ....*....|....*....|....
gi 696227561 338 ISTLAKLNNISNtNLIYAGTTLKI 361
Cdd:COG1388  131 VEELKRWNGLSS-DTIRPGQKLKI 153
LysM smart00257
Lysin motif;
252-294 2.28e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 63.62  E-value: 2.28e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 696227561   252 YTVASGDTLTSIAKAYGTTVSAIATANNISNPDYIYVGEVLTI 294
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 319-361 2.79e-13

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 63.57  E-value: 2.79e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 696227561  319 YTVASGDTLTSIAKAYGVSISTLAKLNNISNTNlIYAGTTLKI 361
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 321-361 2.23e-07

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 46.71  E-value: 2.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 696227561  321 VASGDTLTSIAKAYGVSISTLAKLN-NISNTNLIYAGTTLKI 361
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNPNLIYPGMKIKI 42
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 38-213 9.88e-53

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 175.93  E-value: 9.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  38 ALVTTSSSTSSQAALEAEIEKIEAENTANYSSKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL-ASEYH 116
Cdd:COG1705   96 SANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSN 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 117 NLFGIKGSYN--GQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELLSENSRYSN-LIGETDAATAAEEIYEDGY 193
Cdd:COG1705  176 NLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGaLANAKDYEAFAKALQKAGY 255

                        170       180
                 ....*....|....*....|
gi 696227561 194 ATDPDYTEELEEIINEYNLT 213
Cdd:COG1705  256 ATDPKYADKLISIIESYNLT 275
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 74-216 3.97e-32

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 122.54  E-value: 3.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  74 FLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASEYHNLFGIK--GSYNGQTV---DMPTEEY-YSGAYHEIDD 147
Cdd:NF038016 163 FIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfGSPGPIAVgcrSYATFECsPTGGCFDTTA 242

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 148 YFRVYASDSESITDYEELLSENSRYSNLIGETDAATA-AEEIYEDGYATDPDYTEELEEIINEYNLTAWD 216
Cdd:NF038016 243 TFRAYASAADSFRDHGRFLSVNSRYAPAFAYTDDPDQfAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
71-361 9.62e-31

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 122.88  E-value: 9.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  71 VSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASE-YHNLFGIKGSYNGQTVDMPT-EEYYSGAYHEIDDY 148
Cdd:PRK06347 150 VQSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSApNYNLFGIKGAYNGQSYTKQTlEDDGKGNYYTITAK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 149 FRVYASDSESITDYEELL----SENSRYSNLI--GETDAATAAEEIYEDGYATDPDYTEELEEIINEYNLTAWDSlafky 222
Cdd:PRK06347 230 FRKYPSYHQSLEDYAQVIrkgpSWNPNYYSKVwkSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDS----- 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 223 sGTVVTTTGSTSTSTSSTSSSSTSSSSKSYTVASGDTLTSIAKAYGTTVSAIATANNISNpDYIYVGEVLTIGSSTSTST 302
Cdd:PRK06347 305 -GKTTGGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKS-DFIYPGQKLKVSAGSTTSD 382

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696227561 303 S---------TSSTSSSSTSSSSKSYTVASGDTLTSIAKAYGVSISTLAKLNNIsNTNLIYAGTTLKI 361
Cdd:PRK06347 383 TntskpstgtSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNL-KSDFIYPGQKLKV 449
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 64-214 3.06e-28

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 107.52  E-value: 3.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561    64 TANYSSKVstFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASEYHNLFGIKGSYNGQTVDMPTEEYYSGAYH 143
Cdd:smart00047   3 LAGGSTLE--FVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGGWV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696227561   144 EIDDYFRVYASDSESITDYeELLSENSRYSNLIGETDAATAaeeiyedGYATDPDYTEELEEIINEYNLTA 214
Cdd:smart00047  81 TVKAAFRGYFGEKFIDYAY-VLRGQNPLYKKRWGSNALQTA-------GYATDPDYAKKLIRIIALYDEKL 143
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 74-209 5.02e-28

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 111.10  E-value: 5.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561   74 FLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL----ASEYHNLFGIK--GSYNGQTVDMPTEEYYSGAYHEIDD 147
Cdd:TIGR02541 151 FVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTA 230

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696227561  148 YFRVYASDSESITDYEELLSENSRYSNLIGETDAATAAEEIYEDGYATDPDYTEELEEIINE 209
Cdd:TIGR02541 231 KFRSYSSYEEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQS 292
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
93-207 2.04e-25

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 104.19  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  93 PSLTAAQAILESGWGTS----TLASEYHNLFGIK--GSYNGQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELL 166
Cdd:PRK05684 174 HHLLLAQAALESGWGQReirtADGSPSHNLFGIKadGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLL 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 696227561 167 SENSRYSNLIGETDAATAAEEIYEDGYATDPDYTEELEEII 207
Cdd:PRK05684 254 TNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVI 294
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 69-209 1.16e-22

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 97.12  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  69 SKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL----ASEYHNLFGIKG--SYNGQTVDMPTEEYYSGAY 142
Cdd:PRK12713 179 SHVVDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELrhedGSTSYNLFGIKAgaSWKGKVVNVMTTEYVDGVA 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696227561 143 HEIDDYFRVYASDSESITDYEELLSENSRYSNLIGETDAATAAEEIYEDGYATDPDYTEELEEIINE 209
Cdd:PRK12713 259 QKLVQPFRAYSSYEESFSDYARLIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQ 325
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 80-162 3.11e-22

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 89.55  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561   80 ESAINGWTQYKILPSLTAAQAILESGWGTSTLASEYHNLFGIKGSYNGQtVDMPTEEYYSGAyheiddYFRVYASDSESI 159
Cdd:pfam01832   2 PAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGK-VAYDTDEVTVAA------RFRKYDSVEESI 74


                  ...
gi 696227561  160 TDY 162
Cdd:pfam01832  75 RDY 77
PRK08581 PRK08581
amidase domain-containing protein;
68-216 5.15e-22

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 97.17  E-value: 5.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  68 SSKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTLASE-YHNLFGIKGSYNGQTVDMPTEEYYSGAYHEID 146
Cdd:PRK08581 317 SKDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSpNHNLFGIKGAYEGNSVSFNTLEADGNQLYSIN 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 147 DYFRVYASDSESITDYEELL----------------SENSRYSnligetDAATAAEEIyedgYATDPDYTEELEEIINEY 210
Cdd:PRK08581 397 AGFRKYPSTKESLEDYADLIkngidgnstiykptwkSEAKSYK------DATSHLSKT----YATDPNYAKKLNSIIKHY 466


                 ....*.
gi 696227561 211 NLTAWD 216
Cdd:PRK08581 467 NLTQFD 472
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 69-209 3.94e-21

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 92.76  E-value: 3.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  69 SKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWG----TSTLASEYHNLFGIKG--SYNGQTVDMPTEEYYSGAY 142
Cdd:PRK12712 195 AHVSAFVARMAGPAEAASRASGVPARLIVGQAALESGWGrreiTHADGSTTFNVFGIKAgaNWKGRVAEVTTTEYVDGQP 274

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696227561 143 HEIDDYFRVYASDSESITDYEELLSENSRYSNLIGETDAATAAEEIYEDGYATDPDYTEELEEIINE 209
Cdd:PRK12712 275 QKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHKLVKIMKK 341
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 99-209 1.97e-19

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 87.67  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  99 QAILESGWGTSTL----ASEYHNLFGIKGS--YNGQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELLSENSRY 172
Cdd:PRK12709 201 QAALESGWGKREIrgadGSTSYNVFGIKATkgWTGRTVSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRY 280

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 696227561 173 SNLI-GETDAATAAEEIYEDGYATDPDYTEELEEIINE 209
Cdd:PRK12709 281 AGVLnASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQ 318
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
98-208 1.22e-17

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 83.47  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  98 AQAILESGWGTSTLA--SEYHNLFGIKGS-YNGQTVDMPTEEYYSGAYHEIDDYFRVYASDSESITDYEELLSENSRYSN 174
Cdd:PRK12711 242 AQAALETGWGRRGIGngGDSNNLFGIKATgWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQ 321

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 696227561 175 -LIGETDAATAAEEIYEDGYATDPDYTEELEEIIN 208
Cdd:PRK12711 322 aLQAGTDIKGFARGLQQAGYATDPGYAAKIAAIAN 356
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 250-294 1.13e-14

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 67.51  E-value: 1.13e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 696227561 250 KSYTVASGDTLTSIAKAYGTTVSAIATANNISNPDYIYVGEVLTI 294
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 317-361 2.91e-14

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 66.35  E-value: 2.91e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 696227561 317 KSYTVASGDTLTSIAKAYGVSISTLAKLNNISNTNLIYAGTTLKI 361
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
178-361 1.19e-13

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 67.81  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 178 ETDAATAAEEIYEDGYATDPDYTEELEEIINEYNLTAWDSLAFKYSGTVVTTTGSTSTSTSSTSSSSTSSSSKSYTVASG 257
Cdd:COG1388   12 LLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 258 DTLTSIAKAYGTTVSAiatannisnpdyiyvgevltigsststststsstsssstssSSKSYTVASGDTLTSIAKAYGVS 337
Cdd:COG1388   92 DTLSGIARRYGAAAAP-----------------------------------------SPVTYTVKKGDTLWSIARRYGVS 130

                        170       180
                 ....*....|....*....|....
gi 696227561 338 ISTLAKLNNISNtNLIYAGTTLKI 361
Cdd:COG1388  131 VEELKRWNGLSS-DTIRPGQKLKI 153
LysM smart00257
Lysin motif;
252-294 2.28e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 63.62  E-value: 2.28e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 696227561   252 YTVASGDTLTSIAKAYGTTVSAIATANNISNPDYIYVGEVLTI 294
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 319-361 2.79e-13

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 63.57  E-value: 2.79e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 696227561  319 YTVASGDTLTSIAKAYGVSISTLAKLNNISNTNlIYAGTTLKI 361
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
LysM smart00257
Lysin motif;
319-361 3.26e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 63.23  E-value: 3.26e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 696227561   319 YTVASGDTLTSIAKAYGVSISTLAKLNNISNTNLIYAGTTLKI 361
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 252-294 5.86e-13

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 62.41  E-value: 5.86e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 696227561  252 YTVASGDTLTSIAKAYGTTVSAIATANNISNPDyIYVGEVLTI 294
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKI 42
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 251-352 1.98e-11

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 64.76  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 251 SYTVASGDTLTSIAKAYGTTVSAIATANNISNpDYIYVGEVLTIGSSTSTSTSTSSTSSSstsssskSYTVASGDTLTSI 330
Cdd:PRK10783 345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTLTIGAGSSAQRLANNSDSI-------TYRVRKGDSLSSI 416

                         90       100
                 ....*....|....*....|..
gi 696227561 331 AKAYGVSISTLAKLNNISNTNL 352
Cdd:PRK10783 417 AKRHGVNIKDVMRWNSDTAKNL 438
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 250-294 7.73e-10

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 57.32  E-value: 7.73e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 696227561 250 KSYTVASGDTLTSIAKAY---GTTVSAIATAN--NISNPDYIYVGEVLTI 294
Cdd:COG1652  110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 63-206 4.89e-09

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 56.72  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  63 NTANYSSKVSTFLNEIIESAINGWTQYKILPSLTAAQAILESGWGTSTL----ASEYHNLFGIK-GSYNG-QTVDMPTEE 136
Cdd:PRK12710 122 NSEESLSVVDDFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTrdadGSSSNNLFNIKtGSHSEvESIQVKTTE 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696227561 137 YYSGAYHEIDDYFRVYASDSESITDYEELLSENSRYS-NLIGETDAATAAEEIYEDGYATDPDYTEELEEI 206
Cdd:PRK12710 202 YIADTPIKINASFRKYPSIEHSFHDYVSLIKGSERYQmALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
Bax COG2992
Uncharacterized FlgJ-related protein [General function prediction only];
93-221 2.18e-08

Uncharacterized FlgJ-related protein [General function prediction only];


Pssm-ID: 442231  Cd Length: 253  Bit Score: 54.54  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561  93 PSLTAAQAILESGWGTSTLASEYHNLFGI----KGsyNGqtvdMPTEEYYSGAYHEIddyfRVYASDSESI--------- 159
Cdd:COG2992  121 PSLVLAQAANESGWGTSRFAREGNNLFGQwcfsKG--CG----LVPKQRDEGANHEV----AKFDSPQASVrsymlnlnt 190

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 696227561 160 -TDYEEL--LSENSRYSNliGETDAATAAE--EIY-EDGYAtdpdYTEELEEIINEYNLTAWDSLAFK 221
Cdd:COG2992  191 hPAYKDLrqIRAQLRAEG--KPLTGLALAEglENYsERGEA----YVEELRSMIRYNNLERYDEAQLA 252
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 252-361 6.48e-08

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 51.55  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696227561 252 YTVASGDTLTSIAKAYGTTVSAIATANNISNPDYIYVGEVLTIGSSTSTSTSTSSTSSSSTSSSSKSYTVASGDTLTSIA 331
Cdd:COG1652   45 AGGALAAALPLAAGLAAAVAAAAAAAVLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIA 124

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 696227561 332 KAY---GVSISTLAKLN--NISNTNLIYAGTTLKI 361
Cdd:COG1652  125 KRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 321-361 2.23e-07

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 46.71  E-value: 2.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 696227561  321 VASGDTLTSIAKAYGVSISTLAKLN-NISNTNLIYAGTTLKI 361
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANpQLSNPNLIYPGMKIKI 42
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 318-361 1.17e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 50.12  E-value: 1.17e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 696227561 318 SYTVASGDTLTSIAKAYGVSISTLAKLNNISnTNLIYAGTTLKI 361
Cdd:PRK10783 345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLR-GSKLKVGQTLTI 387
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 252-294 5.46e-06

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 45.68  E-value: 5.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 696227561 252 YTVASGDTLTSIAKAY---GTTVSAIATANN--ISNPDYIYVGEVLTI 294
Cdd:PRK11198  98 YTVKSGDTLSAIAKKVygnANKYNKIFEANKpmLKSPDKIYPGQVLRI 145
PRK10356 PRK10356
protein bax;
91-122 8.21e-05

protein bax;


Pssm-ID: 182404  Cd Length: 274  Bit Score: 43.71  E-value: 8.21e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 696227561  91 ILP-SLTAAQAILESGWGTSTLASEYHNLFGIK 122
Cdd:PRK10356 148 IIPtSMVATMAAAESGWGTSKLARNNNNLFGMK 180
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 317-361 9.14e-04

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 40.81  E-value: 9.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 696227561 317 KSYTVASGDTLTSIAKAYGVSISTLAKL--NNISNTNL--IYAGTTLKI 361
Cdd:COG3061   70 QEYTVQSGDTLSQIFRRLGLSASDLYALlaAEGDAKPLsrLKPGQELRF 118
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
250-294 5.36e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 38.52  E-value: 5.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 696227561 250 KSYTVASGDTLTSIAKAYGTTVSAIATANNISNpDYIYVGEVLTI 294
Cdd:PRK06347 548 KTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTS-NMIHVGQKLTI 591
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
88-122 5.36e-03

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 38.41  E-value: 5.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 696227561  88 QYKILPSLTAAQAILESGWGTSTLAS-------EYHNLFGIK 122
Cdd:COG4193  284 KYGVNPLYLASHALLETGNGTSKLAKgvevngkTYYNLFGIG 325
 
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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