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Conserved domains on  [gi|495540277|ref|WP_008264856|]
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MULTISPECIES: D-alanyl-D-alanine carboxypeptidase family protein [Stenotrophomonas]

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
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];
54-394 6.35e-139

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


:

Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 399.21  E-value: 6.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGagtdgSYSGFPVNQTA 133
Cdd:COG1686   28 AKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGG-----SKMGLKPGEQV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 134 RLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDYP 213
Cdd:COG1686  103 TVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 214 ETYAYNKIKEFQVGN---IKQPNRNLLLWRDGSVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLAL 290
Cdd:COG1686  183 EFYEIFSTKEFTFPNgrgITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 291 LNWGFrffethrlyepgkavaehkvwkgttdkvqlgvaqpmlvsvPRGRYndLKPSIDVPKTLEAPFTAGQQVGTVKVTL 370
Cdd:COG1686  263 LDYGF----------------------------------------PKGEA--LKAEVVLDGPLKAPVKKGQVVGTLVVTL 300
                        330       340
                 ....*....|....*....|....
gi 495540277 371 DGKVIAEAPLVAVAAVEQAGFFKR 394
Cdd:COG1686  301 DGKTIAEVPLVAAEDVEKAGFFSR 324
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
54-394 6.35e-139

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 399.21  E-value: 6.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGagtdgSYSGFPVNQTA 133
Cdd:COG1686   28 AKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGG-----SKMGLKPGEQV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 134 RLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDYP 213
Cdd:COG1686  103 TVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 214 ETYAYNKIKEFQVGN---IKQPNRNLLLWRDGSVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLAL 290
Cdd:COG1686  183 EFYEIFSTKEFTFPNgrgITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 291 LNWGFrffethrlyepgkavaehkvwkgttdkvqlgvaqpmlvsvPRGRYndLKPSIDVPKTLEAPFTAGQQVGTVKVTL 370
Cdd:COG1686  263 LDYGF----------------------------------------PKGEA--LKAEVVLDGPLKAPVKKGQVVGTLVVTL 300
                        330       340
                 ....*....|....*....|....
gi 495540277 371 DGKVIAEAPLVAVAAVEQAGFFKR 394
Cdd:COG1686  301 DGKTIAEVPLVAAEDVEKAGFFSR 324
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
54-405 1.18e-120

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 355.84  E-value: 1.18e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGAGTDGSYSGF--PVNQ 131
Cdd:PRK10001  39 ARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFlkPGDQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 132 TArLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRD 211
Cdd:PRK10001 119 VS-VADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 212 YPETYAYNKIKEFQVGNIKQPNRNLLLWRDG-SVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLAL 290
Cdd:PRK10001 198 VPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKL 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 291 LNWGFRFFETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVPK-TLEAPFTAGQQVGTVKVT 369
Cdd:PRK10001 278 LTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEpQLTAPLKKGQVVGTIDFQ 357
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 495540277 370 LDGKVIAEAPLVAVAAVEQAGFFKRLWD----SFWMWWES 405
Cdd:PRK10001 358 LNGKSIEQRPLIVMENVEEGGFFSRMWDfvmmKFHQWFGS 397
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
54-277 5.80e-87

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 263.86  E-value: 5.80e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277   54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGagtDGSYSGF-PVNQT 132
Cdd:pfam00768   8 AKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGN---PGSSNIFlKPGSQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  133 ARLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDY 212
Cdd:pfam00768  85 VSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKALIKDL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495540277  213 PETYAYNKIKEF---QVGNIKQPNRNLLLWRDG-SVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGG 277
Cdd:pfam00768 165 PEELSITKEKSFtfrGINKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGA 233
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
298-388 1.17e-29

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: 110.00  E-value: 1.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277   298 FETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVP-KTLEAPFTAGQQVGTVKVTLDGKVIA 376
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDkPELEAPIKKGQVVGTLVVTLDGKLIG 80
                           90
                   ....*....|..
gi 495540277   377 EAPLVAVAAVEQ 388
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
54-394 6.35e-139

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 399.21  E-value: 6.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGagtdgSYSGFPVNQTA 133
Cdd:COG1686   28 AKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGG-----SKMGLKPGEQV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 134 RLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDYP 213
Cdd:COG1686  103 TVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 214 ETYAYNKIKEFQVGN---IKQPNRNLLLWRDGSVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLAL 290
Cdd:COG1686  183 EFYEIFSTKEFTFPNgrgITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 291 LNWGFrffethrlyepgkavaehkvwkgttdkvqlgvaqpmlvsvPRGRYndLKPSIDVPKTLEAPFTAGQQVGTVKVTL 370
Cdd:COG1686  263 LDYGF----------------------------------------PKGEA--LKAEVVLDGPLKAPVKKGQVVGTLVVTL 300
                        330       340
                 ....*....|....*....|....
gi 495540277 371 DGKVIAEAPLVAVAAVEQAGFFKR 394
Cdd:COG1686  301 DGKTIAEVPLVAAEDVEKAGFFSR 324
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
54-405 1.18e-120

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 355.84  E-value: 1.18e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGAGTDGSYSGF--PVNQ 131
Cdd:PRK10001  39 ARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFlkPGDQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 132 TArLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRD 211
Cdd:PRK10001 119 VS-VADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 212 YPETYAYNKIKEFQVGNIKQPNRNLLLWRDG-SVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLAL 290
Cdd:PRK10001 198 VPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKL 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 291 LNWGFRFFETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVPK-TLEAPFTAGQQVGTVKVT 369
Cdd:PRK10001 278 LTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEpQLTAPLKKGQVVGTIDFQ 357
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 495540277 370 LDGKVIAEAPLVAVAAVEQAGFFKRLWD----SFWMWWES 405
Cdd:PRK10001 358 LNGKSIEQRPLIVMENVEEGGFFSRMWDfvmmKFHQWFGS 397
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
54-397 4.58e-113

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 336.44  E-value: 4.58e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGAGTDGSYSGF--PVNQ 131
Cdd:PRK10793  46 AESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFlkPGMQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 132 TArLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRD 211
Cdd:PRK10793 126 VP-VSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRD 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 212 YPETYAYNKIKEFQVGNIKQPNRNLLLWRDG-SVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLAL 290
Cdd:PRK10793 205 VPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSlNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKL 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 291 LNWGFRFFETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVPKT-LEAPFTAGQQVGTVKVT 369
Cdd:PRK10793 285 LTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTSeLHAPLQKNQVVGTINFQ 364
                        330       340
                 ....*....|....*....|....*...
gi 495540277 370 LDGKVIAEAPLVAVAAVEQAGFFKRLWD 397
Cdd:PRK10793 365 LDGKTIEQRPLVVLQEIPEGNFFGKIID 392
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
56-399 2.74e-103

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 310.98  E-value: 2.74e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  56 AWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGAGTDGSYSGFpVNQTARL 135
Cdd:PRK11397  38 SWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPVFVGSSLMF-LKEGDRV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 136 --EDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDYP 213
Cdd:PRK11397 117 svRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEP 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 214 ETYAYNKIKEFQVGNIKQPNRNLLLW-RDGSVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLALLN 292
Cdd:PRK11397 197 EFYHMYSEKSLTWNGITQQNRNGLLWdKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLR 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 293 WGFRFFETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPS--IDvPKTLEAPFTAGQQVGTVKVTL 370
Cdd:PRK11397 277 WGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKyvLD-GKELEAPISAHQRVGEIELYD 355
                        330       340
                 ....*....|....*....|....*....
gi 495540277 371 DGKVIAEAPLVAVAAVEQAGFFKRLWDSF 399
Cdd:PRK11397 356 RDKQVAHWPLVTLESVGEGGMFSRLSDYF 384
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
54-277 5.80e-87

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 263.86  E-value: 5.80e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277   54 SKAWVLMDYATGQVLAGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGagtDGSYSGF-PVNQT 132
Cdd:pfam00768   8 AKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGN---PGSSNIFlKPGSQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  133 ARLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDY 212
Cdd:pfam00768  85 VSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKALIKDL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495540277  213 PETYAYNKIKEF---QVGNIKQPNRNLLLWRDG-SVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGG 277
Cdd:pfam00768 165 PEELSITKEKSFtfrGINKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGA 233
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
298-388 1.12e-29

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: 110.38  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  298 FETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVPKTLEAPFTAGQQVGTVKVTLDGKVIAE 377
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKPLEAPIKKGQVVGKLEVYLDGKLIGE 80
                          90
                  ....*....|.
gi 495540277  378 APLVAVAAVEQ 388
Cdd:pfam07943  81 VPLVAKEDVEE 91
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
298-388 1.17e-29

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: 110.00  E-value: 1.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277   298 FETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVP-KTLEAPFTAGQQVGTVKVTLDGKVIA 376
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDkPELEAPIKKGQVVGTLVVTLDGKLIG 80
                           90
                   ....*....|..
gi 495540277   377 EAPLVAVAAVEQ 388
Cdd:smart00936  81 EVPLVALEDVEK 92
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
59-293 9.26e-16

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 77.41  E-value: 9.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  59 LMDYATGQVLAGENVHEQLAPASITKVMTSYViaaeVKNGKVRADDQVMMSERAWREggagTDGSYSGFPVNQTARLEDM 138
Cdd:PRK11669  46 VVDLNTNKVIYSSNPDLVVPIASITKLMTAMV----VLDAKLPLDEKLKVDISQTPE----MKGVYSRVRLNSEISRKDM 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 139 EKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQgHHSTAYDLALLGRAmVRDYPETYAY 218
Cdd:PRK11669 118 LLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPTGLSIH-NVSTARDLTKLLIA-SKQYPLIGQL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277 219 NKIKEFQVgNIKQP-------NRNLLLWRDG-SVDGIKTGHTSEAGYCLMSSAQRGdQRLIAVVLGGASEKQR--ADDSl 288
Cdd:PRK11669 196 STTREKTA-TFRKPnytlpfrNTNHLVYRDNwNIQLTKTGFTNAAGHCLVMRTVIN-NRPVALVVLDAFGKYThfADAS- 272

                 ....*
gi 495540277 289 ALLNW 293
Cdd:PRK11669 273 RLRTW 277
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
57-185 1.83e-06

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: 48.42  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277   57 WVLMDYATGQVLaGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAwREGGAGTdgsYSGFPVNQTARLE 136
Cdd:pfam13354   2 IYVRDLDTGEEL-GINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAED-KVGGSGI---LQYLPDGSQLSLR 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 495540277  137 DMEKGMAIQSGNDAAIALAEHVAGSEeafaslMNSYAAKIGMKDSHFVN 185
Cdd:pfam13354  77 DLLTLMIAVSDNTATNLLIDRLGLEA------VNARLRALGLRDTRLRR 119
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
59-211 1.76e-05

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 46.04  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495540277  59 LMDYATGQVLaGENVHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSErAWREGGAGTdgsYSGFPVNQTARLEDM 138
Cdd:COG2367   39 VLDLDTGETV-GINADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTP-EDLVGGSGI---LQKLPDGTGLTLREL 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495540277 139 EKGMAIQSGNDAAIALAEHVaGSEEafaslMNSYAAKIGMKDSHFVN----AHGLTAQG-HHSTAYDLALLGRAMVRD 211
Cdd:COG2367  114 AELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTRLDRkepdLNELPGDGrNTTTPRDMARLLAALYRG 185
 
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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