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Conserved domains on  [gi|493690390|ref|WP_006640426|]
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MULTISPECIES: D-alanyl-D-alanine carboxypeptidase family protein [Bacillus]

Protein Classification

D-alanyl-D-alanine carboxypeptidase family protein( domain architecture ID 11447584)

D-alanyl-D-alanine carboxypeptidase family protein may remove C-terminal D-alanyl residues from sugar-peptide cell wall precursors

CATH:  3.40.710.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S11
PubMed:  1741619|8439290|7845208
SCOP:  3001604

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
14-415 3.39e-113

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 335.27  E-value: 3.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  14 MAFAIVVGAF-SPMSNAKAANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKY 92
Cdd:COG1686    1 MKKLLLLALLlLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  93 TPDDYVYEISqdrsLSNVPLRKDGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFVNAT 172
Cdd:COG1686   81 TVSEEAARTG----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 173 GLEnkdlhgkhpsgtsaNEENEVSARDMAILADHLVNDYPEILDTASIAKTKFREGtdDEMDMPNWNFMLKglvqEYKGV 252
Cdd:COG1686  157 GLP--------------DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNRLLG----RYPGV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 253 DGLKTGSTDSAGSCFTATAKRNGMRVISVVLNAKGnlHTARFDATKKMLDYAFDNfsmkelyakgaqvkgnetvkvdqgk 332
Cdd:COG1686  217 DGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGFPK------------------------- 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 333 eqevgiitekalsipvkngdEKKYKAKVTLDkKELSAPVKKGEKVGTLTASYTGDEkdygfigsdISGVKLVTKEADEKA 412
Cdd:COG1686  270 --------------------GEALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKT---------IAEVPLVAAEDVEKA 319


                 ...
gi 493690390 413 NWF 415
Cdd:COG1686  320 GFF 322
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
14-415 3.39e-113

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 335.27  E-value: 3.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  14 MAFAIVVGAF-SPMSNAKAANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKY 92
Cdd:COG1686    1 MKKLLLLALLlLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  93 TPDDYVYEISqdrsLSNVPLRKDGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFVNAT 172
Cdd:COG1686   81 TVSEEAARTG----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 173 GLEnkdlhgkhpsgtsaNEENEVSARDMAILADHLVNDYPEILDTASIAKTKFREGtdDEMDMPNWNFMLKglvqEYKGV 252
Cdd:COG1686  157 GLP--------------DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNRLLG----RYPGV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 253 DGLKTGSTDSAGSCFTATAKRNGMRVISVVLNAKGnlHTARFDATKKMLDYAFDNfsmkelyakgaqvkgnetvkvdqgk 332
Cdd:COG1686  217 DGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGFPK------------------------- 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 333 eqevgiitekalsipvkngdEKKYKAKVTLDkKELSAPVKKGEKVGTLTASYTGDEkdygfigsdISGVKLVTKEADEKA 412
Cdd:COG1686  270 --------------------GEALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKT---------IAEVPLVAAEDVEKA 319


                 ...
gi 493690390 413 NWF 415
Cdd:COG1686  320 GFF 322
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
35-286 2.17e-84

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 258.47  E-value: 2.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   35 PINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKYTPDDYVYEISQDRSlSNVPLRK 114
Cdd:pfam00768   3 APEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  115 DGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFVNATGLENKDLHGkhpsgtsaneene 194
Cdd:pfam00768  82 GSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYS------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  195 vSARDMAILADHLVNDYPEILDTASIAKTKFREgtddemdMPNWNFMLKGLVQEYKG--VDGLKTGSTDSAGSCFTATAK 272
Cdd:pfam00768 149 -SARDMAILAKALIKDLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASAT 220

                         250
                  ....*....|....
gi 493690390  273 RNGMRVISVVLNAK 286
Cdd:pfam00768 221 KGGMRLISVVMGAF 234
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
24-441 1.34e-55

serine-type D-Ala-D-Ala carboxypeptidase;


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 189.43  E-value: 1.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  24 SPMSNAKAANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKYT--PDDYVYEI 101
Cdd:PRK10001  23 PTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTvgKDAWATGN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 102 SQDRSLSNVPLRKDGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFvnatglenKDLHG 181
Cdd:PRK10001 103 PALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF--------QTVHG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 182 KHPSGTSAneenevSARDMAILADHLVNDYPEildtaSIAKTKFREGTDDEMDMPNWNFMlkgLVQEYKGVDGLKTGSTD 261
Cdd:PRK10001 175 LDAPGQFS------TARDMALLGKALIHDVPE-----EYAIHKEKEFTFNKIRQPNRNRL---LWSSNLNVDGMKTGTTA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 262 SAGSCFTATAKRNGMRVISVVLNAKGNlhTARFDATKKMLDYAFdnfsmkELYAKGAQVKGNETV---KVDQGKEQEVGI 338
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGF------RFFETVTPIKPDATFvtqRVWFGDKSEVNL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 339 ITEKALSIPVKNGDEKKYKAKVTLDKKELSAPVKKGEKVGTLtasytgdekDYGFIGSDISGVKLVTKEADEKanwfvlt 418
Cdd:PRK10001 313 GAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTI---------DFQLNGKSIEQRPLIVMENVEE------- 376

                        410       420
                 ....*....|....*....|...
gi 493690390 419 mrsiGGFFAGIWNSIVDMVTGWF 441
Cdd:PRK10001 377 ----GGFFSRMWDFVMMKFHQWF 395
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 308-411 3.50e-20

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 84.58  E-value: 3.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   308 FSMKELYAKGAQVKgneTVKVDQGKEQEVGIITEKALSIPVKNGDEKKYKAKVTLDKKELSAPVKKGEKVGTLTasYTGD 387
Cdd:smart00936   1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLV--VTLD 75

                           90       100
                   ....*....|....*....|....
gi 493690390   388 EKdygfigsDISGVKLVTKEADEK 411
Cdd:smart00936  76 GK-------LIGEVPLVALEDVEK 92
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
14-415 3.39e-113

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 335.27  E-value: 3.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  14 MAFAIVVGAF-SPMSNAKAANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKY 92
Cdd:COG1686    1 MKKLLLLALLlLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  93 TPDDYVYEISqdrsLSNVPLRKDGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFVNAT 172
Cdd:COG1686   81 TVSEEAARTG----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 173 GLEnkdlhgkhpsgtsaNEENEVSARDMAILADHLVNDYPEILDTASIAKTKFREGtdDEMDMPNWNFMLKglvqEYKGV 252
Cdd:COG1686  157 GLP--------------DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNRLLG----RYPGV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 253 DGLKTGSTDSAGSCFTATAKRNGMRVISVVLNAKGnlHTARFDATKKMLDYAFDNfsmkelyakgaqvkgnetvkvdqgk 332
Cdd:COG1686  217 DGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGFPK------------------------- 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 333 eqevgiitekalsipvkngdEKKYKAKVTLDkKELSAPVKKGEKVGTLTASYTGDEkdygfigsdISGVKLVTKEADEKA 412
Cdd:COG1686  270 --------------------GEALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKT---------IAEVPLVAAEDVEKA 319


                 ...
gi 493690390 413 NWF 415
Cdd:COG1686  320 GFF 322
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
35-286 2.17e-84

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 258.47  E-value: 2.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   35 PINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKYTPDDYVYEISQDRSlSNVPLRK 114
Cdd:pfam00768   3 APEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  115 DGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFVNATGLENKDLHGkhpsgtsaneene 194
Cdd:pfam00768  82 GSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYS------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  195 vSARDMAILADHLVNDYPEILDTASIAKTKFREgtddemdMPNWNFMLKGLVQEYKG--VDGLKTGSTDSAGSCFTATAK 272
Cdd:pfam00768 149 -SARDMAILAKALIKDLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASAT 220

                         250
                  ....*....|....
gi 493690390  273 RNGMRVISVVLNAK 286
Cdd:pfam00768 221 KGGMRLISVVMGAF 234
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
24-441 1.34e-55

serine-type D-Ala-D-Ala carboxypeptidase;


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 189.43  E-value: 1.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  24 SPMSNAKAANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQKYT--PDDYVYEI 101
Cdd:PRK10001  23 PTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTvgKDAWATGN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 102 SQDRSLSNVPLRKDGSYTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKELGMKNFKFvnatglenKDLHG 181
Cdd:PRK10001 103 PALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF--------QTVHG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 182 KHPSGTSAneenevSARDMAILADHLVNDYPEildtaSIAKTKFREGTDDEMDMPNWNFMlkgLVQEYKGVDGLKTGSTD 261
Cdd:PRK10001 175 LDAPGQFS------TARDMALLGKALIHDVPE-----EYAIHKEKEFTFNKIRQPNRNRL---LWSSNLNVDGMKTGTTA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 262 SAGSCFTATAKRNGMRVISVVLNAKGNlhTARFDATKKMLDYAFdnfsmkELYAKGAQVKGNETV---KVDQGKEQEVGI 338
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGF------RFFETVTPIKPDATFvtqRVWFGDKSEVNL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 339 ITEKALSIPVKNGDEKKYKAKVTLDKKELSAPVKKGEKVGTLtasytgdekDYGFIGSDISGVKLVTKEADEKanwfvlt 418
Cdd:PRK10001 313 GAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTI---------DFQLNGKSIEQRPLIVMENVEE------- 376

                        410       420
                 ....*....|....*....|...
gi 493690390 419 mrsiGGFFAGIWNSIVDMVTGWF 441
Cdd:PRK10001 377 ----GGFFSRMWDFVMMKFHQWF 395
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
7-415 3.81e-42

serine-type D-Ala-D-Ala carboxypeptidase DacD;


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 153.05  E-value: 3.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   7 KQLIMLVMAFAIVVGAFSPMSNAKAANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKV 86
Cdd:PRK11397   3 RRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  87 kwdqkyTPDDYVyEISQDRSLSNVPLRKDGSY---------TVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKK 157
Cdd:PRK11397  83 ------TPDDIV-TVGRDAWAKDNPVFVGSSLmflkegdrvSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 158 AKELGMKNFKFVNATGLenkDLHGKHPsgtsaneenevSARDMAILADHLVNDYPEILDTASiaktkfregtddEMDMpN 237
Cdd:PRK11397 156 VEKLHLKDTHFETVHGL---DAPGQHS-----------SAYDLAVLSRAIIHGEPEFYHMYS------------EKSL-T 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 238 WNfmlkGLVQEYKG---------VDGLKTGSTDSAGSCFTATAKRNGMRVISVVLNAKGNlhTARFDATKKMLDYAFDNF 308
Cdd:PRK11397 209 WN----GITQQNRNgllwdktmnVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSA--KGREEQARKLLRWGQQNF 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 309 SMKELYAKGAQVkGNEtvKVDQGKEQEVGIITEKALSIPVKNGDEKKYKAKVTLDKKELSAPVKKGEKVGTLTAsYTGDE 388
Cdd:PRK11397 283 TTVQILHRGKKV-GTE--RIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVGEIEL-YDRDK 358

                        410       420
                 ....*....|....*....|....*..
gi 493690390 389 KdygfigsdISGVKLVTKEADEKANWF 415
Cdd:PRK11397 359 Q--------VAHWPLVTLESVGEGGMF 377
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 1-441 1.12e-41

D-alanyl-D-alanine carboxypeptidase fraction A; Provisional


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 152.32  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   1 MKSKRIKQLIMLVMAFAIVVGAFSPMSNAKAANDPI------NVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTE 74
Cdd:PRK10793   1 MKTIFSARIMKRLALTTALCTAFISAAHADDLNIKTmipgvpQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  75 YLLLEAIHEGKVKwdqkytPDDYVyEISQDRSLSNVPLRKDGSY---------TVKELYQATAIYSANAAAIALSEIVAG 145
Cdd:PRK10793  81 YVIGQAMKAGKFK------ETDLV-TVGNDAWATGNPVFKGSSLmflkpgmqvPVSQLIRGINLQSGNDACVAMADYVAG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 146 SESNFVELMNKKAKELGMKNFKFVNATGLenkDLHGKHPsgtsaneenevSARDMAILADHLVNDYPeilDTASIAKTKf 225
Cdd:PRK10793 154 SQDAFVGLMNSYVNALGLKNTHFQTVHGL---DADGQYS-----------SARDMALIGQALIRDVP---NEYAIYKEK- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 226 rEGTDDEMDMPNWNfmlkGLVQEYK-GVDGLKTGSTDSAGSCFTATAKRNGMRVISVVLNakGNLHTARFDATKKMLDYA 304
Cdd:PRK10793 216 -EFTFNGIRQLNRN----GLLWDNSlNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMG--GRTFKGRETESKKLLTWG 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 305 FDNFSMKELYAKGAQVkGNETVKVDQGKEQEVGIITEKALSIPvkNGDEKKYKAKVTLDKKELSAPVKKGEKVGTLtasy 384
Cdd:PRK10793 289 FRFFETVNPLKVGKEF-ASEPVWFGDSDRASLGVDKDVYLTIP--RGRMKDLKASYVLNTSELHAPLQKNQVVGTI---- 361

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493690390 385 tgdekDYGFIGSDISGVKLVtkeadekanwfVLTMRSIGGFFAGIWNSIVDMVTGWF 441
Cdd:PRK10793 362 -----NFQLDGKTIEQRPLV-----------VLQEIPEGNFFGKIIDYIKLMFHHWF 402
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 9-298 2.20e-25

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 105.53  E-value: 2.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   9 LIMLVMAFAIVvgAFSPMSNAK-----AANDPINVNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAihe 83
Cdd:PRK11669   7 LLSLLLLLAGV--PFAPQAVAKtaaatTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  84 gKVKWDQKYTPDdyvyeISQDRSLSNVPLR-KDGS-YTVKELYQATAIYSANAAAIALSEIVAGSESNFVELMNKKAKEL 161
Cdd:PRK11669  82 -KLPLDEKLKVD-----ISQTPEMKGVYSRvRLNSeISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKAL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 162 GMKNFKFVNATGLenkdlhgkhpsgtsaNEENEVSARDMAIL--ADHlvnDYPEI-------LDTASIAKTK----FREg 228
Cdd:PRK11669 156 GMTNTRYVEPTGL---------------SIHNVSTARDLTKLliASK---QYPLIgqlsttrEKTATFRKPNytlpFRN- 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493690390 229 TDDEMDMPNWNFMLKglvqeykgvdglKTGSTDSAGSCFTATAKRNGMRVISVVLNAKGNL-HTArfDATK 298
Cdd:PRK11669 217 TNHLVYRDNWNIQLT------------KTGFTNAAGHCLVMRTVINNRPVALVVLDAFGKYtHFA--DASR 273
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 308-411 3.50e-20

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 84.58  E-value: 3.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   308 FSMKELYAKGAQVKgneTVKVDQGKEQEVGIITEKALSIPVKNGDEKKYKAKVTLDKKELSAPVKKGEKVGTLTasYTGD 387
Cdd:smart00936   1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLV--VTLD 75

                           90       100
                   ....*....|....*....|....
gi 493690390   388 EKdygfigsDISGVKLVTKEADEK 411
Cdd:smart00936  76 GK-------LIGEVPLVALEDVEK 92
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 308-411 1.14e-17

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 429749 [Multi-domain]  Cd Length: 91  Bit Score: 77.63  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  308 FSMKELYAKGAQVKgneTVKVDQGKEQEVGIITEKALSIPVKNGDEKKYKAKVTLdKKELSAPVKKGEKVGTLTasytgd 387
Cdd:pfam07943   1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTL-KKPLEAPIKKGQVVGKLE------ 70

                          90       100
                  ....*....|....*....|....
gi 493690390  388 ekdYGFIGSDISGVKLVTKEADEK 411
Cdd:pfam07943  71 ---VYLDGKLIGEVPLVAKEDVEE 91
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
15-219 1.68e-10

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 61.45  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  15 AFAIVVGAFSPMSNAKAANDPIN-----VNAKAAILIEASSGKVLYSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWD 89
Cdd:COG2367    3 LLALLLLAAAAAAPASALEAELAaleaaLGGRVGVYVLDLDTGETVGINADERFPAASTFKLPVLAAVLRQVDAGKLSLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  90 QK--YTPDDYVYE--ISQDrslsnvpLRKDGSYTVKELYQATAIYSANAAAIALSEIVAGSEsnfvelMNKKAKELGMKN 165
Cdd:COG2367   83 ERvtLTPEDLVGGsgILQK-------LPDGTGLTLRELAELMITVSDNTATNLLLRLLGPDA------VNAFLRSLGLTD 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493690390 166 FKFVNATGlenkDLHGKHPSGTsaneeNEVSARDMAILADHLVNdyPEILDTAS 219
Cdd:COG2367  150 TRLDRKEP----DLNELPGDGR-----NTTTPRDMARLLAALYR--GELLSPES 192
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 55-228 5.63e-10

Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 463854 [Multi-domain]  Cd Length: 215  Bit Score: 58.83  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390   55 YSKNADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQK--YTPDDYVyeisqDRSLSNVPLRKDGSYTVKELYQATAIYSA 132
Cdd:pfam13354  13 LGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERltVTAEDKV-----GGSGILQYLPDGSQLSLRDLLTLMIAVSD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  133 NAAAIALSEIVAGSEsnfvelMNKKAKELGMKNfkfvnaTGLENKDLhgkHPSGTSANEENEVSARDMAILADHLVND-- 210
Cdd:pfam13354  88 NTATNLLIDRLGLEA------VNARLRALGLRD------TRLRRKLP---DLRAADKGGTNTTTARDMAKLLEALYRGel 152

                         170       180
                  ....*....|....*....|...
gi 493690390  211 -----YPEILDtaSIAKTKFREG 228
Cdd:pfam13354 153 lspesTDRLLD--ILSRQQFRDR 173
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
42-306 5.95e-07

CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 51.22  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390  42 AAILIeASSGKVLYSK-------------NADQRLPVASMAKMMTEYLLLEAIHEGKVKWDQ---KYTPD----DYVYE- 100
Cdd:COG1680   35 AAVAV-VRDGKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDDpvsKYLPEfklpDDAKRd 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 101 ------------ISQDRSLSNVPLRKDGSYTVKELYQATA------------IYSaNAAAIALSEIVAG-SESNFVELMN 155
Cdd:COG1680  114 itvrhllthtsgLPDYEPDPYDAADVARPYTPDDLLARLAalpllfepgtrfSYS-NLGYDLLGEIIERvTGQPLEDYLR 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 156 KK-AKELGMKNFKFVNATGLENKDLHGKHPSGTSANEENEV-----------SARDMAILADHLVN----DYPEILDTAS 219
Cdd:COG1680  193 ERiFEPLGMTDTGFGLPDAEAARLAPGYEADGEVHDAPAWLgavagagglfsTARDLARFGQALLNggewDGKRLLSPET 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493690390 220 IAKTkFREGTDDEMDMPNWnfmlkGL---VQEYKGVDGL-KTGSTDSAGSCFTATAKRNgmRVISVVLNAKGNLHTARFD 295
Cdd:COG1680  273 LAEM-TTPQVPSGDAGGGY-----GLgwwLNDDGGSGSFgHGGATPGFSTFLWVDPERG--LGVVVLTNRDDPGAGDRAA 344

                        330
                 ....*....|.
gi 493690390 296 ATKKMLDYAFD 306
Cdd:COG1680  345 LLEALLAALLG 355
 
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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