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Conserved domains on  [gi|521994452|ref|WP_020505723|]
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D-alanyl-D-alanine carboxypeptidase family protein [Lamprocystis purpurea]

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];
53-389 4.58e-143

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


:

Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 409.61  E-value: 4.58e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTGGSKMFVEVGKRVGLED 132
Cdd:COG1686   27 AAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVED 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 133 LLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIREFPQYYV 212
Cdd:COG1686  107 LLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 213 WDGTKEYEYN---GIKQHNRNRLLWRDSTVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLELLNYG 289
Cdd:COG1686  187 IFSTKEFTFPngrGITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 290 FrfyeshrlypggepvkslrvwkgdreevpigpardvlatiPRGryAELSARMDQAPTLTAPIAQGTRLGDIVVTLAGVE 369
Cdd:COG1686  267 F----------------------------------------PKG--EALKAEVVLDGPLKAPVKKGQVVGTLVVTLDGKT 304

                        330       340
                 ....*....|....*....|
gi 521994452 370 ITRVPLVALEAVAEGGLWER 389
Cdd:COG1686  305 IAEVPLVAAEDVEKAGFFSR 324
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
53-389 4.58e-143

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 409.61  E-value: 4.58e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTGGSKMFVEVGKRVGLED 132
Cdd:COG1686   27 AAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVED 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 133 LLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIREFPQYYV 212
Cdd:COG1686  107 LLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 213 WDGTKEYEYN---GIKQHNRNRLLWRDSTVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLELLNYG 289
Cdd:COG1686  187 IFSTKEFTFPngrGITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 290 FrfyeshrlypggepvkslrvwkgdreevpigpardvlatiPRGryAELSARMDQAPTLTAPIAQGTRLGDIVVTLAGVE 369
Cdd:COG1686  267 F----------------------------------------PKG--EALKAEVVLDGPLKAPVKKGQVVGTLVVTLDGKT 304

                        330       340
                 ....*....|....*....|
gi 521994452 370 ITRVPLVALEAVAEGGLWER 389
Cdd:COG1686  305 IAEVPLVAAEDVEKAGFFSR 324
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
53-398 4.38e-113

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 336.19  E-value: 4.38e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTG------GSKMFVEVGK 126
Cdd:PRK10001  38 DARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGnpalrgSSVMFLKPGD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 127 RVGLEDLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIRE 206
Cdd:PRK10001 118 QVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 207 FPQYYVWDGTKEYEYNGIKQHNRNRLLWRDS-TVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLEL 285
Cdd:PRK10001 198 VPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKL 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 286 LNYGFRFYESHrlypggEPVK------SLRVWKGDREEVPIGPARDVLATIPRGRYAELSARMD-QAPTLTAPIAQGTRL 358
Cdd:PRK10001 278 LTWGFRFFETV------TPIKpdatfvTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTlTEPQLTAPLKKGQVV 351

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 521994452 359 GDIVVTLAGVEITRVPLVALEAVAEGGLWERIRDTVL----QWF 398
Cdd:PRK10001 352 GTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMmkfhQWF 395
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
53-273 1.03e-91

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 275.80  E-value: 1.03e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452   53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTGG---SKMFVEVGKRVG 129
Cdd:pfam00768   7 AAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLKPGSQVS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  130 LEDLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIREFPQ 209
Cdd:pfam00768  87 VKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKALIKDLPE 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  210 yyVWDGTKEYEY-----NGIKQHNRNRLLWRDS-TVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAK 273
Cdd:pfam00768 167 --ELSITKEKSFtfrgiNKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 293-383 3.13e-27

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: 103.45  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452   293 YESHRLYPGGEPVKSLRVWKGDREEVPIGPARDVLATIPRGRYAELSARMD-QAPTLTAPIAQGTRLGDIVVTLAGVEIT 371
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVlDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 521994452   372 RVPLVALEAVAE 383
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
53-389 4.58e-143

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 409.61  E-value: 4.58e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTGGSKMFVEVGKRVGLED 132
Cdd:COG1686   27 AAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVED 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 133 LLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIREFPQYYV 212
Cdd:COG1686  107 LLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 213 WDGTKEYEYN---GIKQHNRNRLLWRDSTVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLELLNYG 289
Cdd:COG1686  187 IFSTKEFTFPngrGITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 290 FrfyeshrlypggepvkslrvwkgdreevpigpardvlatiPRGryAELSARMDQAPTLTAPIAQGTRLGDIVVTLAGVE 369
Cdd:COG1686  267 F----------------------------------------PKG--EALKAEVVLDGPLKAPVKKGQVVGTLVVTLDGKT 304

                        330       340
                 ....*....|....*....|
gi 521994452 370 ITRVPLVALEAVAEGGLWER 389
Cdd:COG1686  305 IAEVPLVAAEDVEKAGFFSR 324
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
53-398 4.38e-113

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 336.19  E-value: 4.38e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTG------GSKMFVEVGK 126
Cdd:PRK10001  38 DARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGnpalrgSSVMFLKPGD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 127 RVGLEDLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIRE 206
Cdd:PRK10001 118 QVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 207 FPQYYVWDGTKEYEYNGIKQHNRNRLLWRDS-TVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLEL 285
Cdd:PRK10001 198 VPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKL 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 286 LNYGFRFYESHrlypggEPVK------SLRVWKGDREEVPIGPARDVLATIPRGRYAELSARMD-QAPTLTAPIAQGTRL 358
Cdd:PRK10001 278 LTWGFRFFETV------TPIKpdatfvTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTlTEPQLTAPLKKGQVV 351

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 521994452 359 GDIVVTLAGVEITRVPLVALEAVAEGGLWERIRDTVL----QWF 398
Cdd:PRK10001 352 GTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMmkfhQWF 395
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 53-398 3.78e-100

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 303.31  E-value: 3.78e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTG------GSKMFVEVGK 126
Cdd:PRK10793  45 DAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGnpvfkgSSLMFLKPGM 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 127 RVGLEDLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIRE 206
Cdd:PRK10793 125 QVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRD 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 207 FPQYYVWDGTKEYEYNGIKQHNRNRLLWRDS-TVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLEL 285
Cdd:PRK10793 205 VPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSlNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKL 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 286 LNYGFRFYESHRLYPGGEPVKSLRVWKGDREEVPIGPARDVLATIPRGRYAELSAR-MDQAPTLTAPIAQGTRLGDIVVT 364
Cdd:PRK10793 285 LTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASyVLNTSELHAPLQKNQVVGTINFQ 364

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 521994452 365 LAGVEITRVPLVALEAVAEGGLWERIRDTVL----QWF 398
Cdd:PRK10793 365 LDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKlmfhHWF 402
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
53-392 2.15e-93

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 285.56  E-value: 2.15e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRT------GGSKMFVEVGK 126
Cdd:PRK11397  35 DAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKdnpvfvGSSLMFLKEGD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 127 RVGLEDLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIRE 206
Cdd:PRK11397 115 RVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHG 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 207 FPQYYVWDGTKEYEYNGIKQHNRNRLLWrDST--VDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAKNPEARASASLE 284
Cdd:PRK11397 195 EPEFYHMYSEKSLTWNGITQQNRNGLLW-DKTmnVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARK 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 285 LLNYGFRFYESHRLYPGGEPVKSLRVWKGDREEVPIGPARDVLATIPRGRYAELSAR--MDQaPTLTAPIAQGTRLGDIV 362
Cdd:PRK11397 274 LLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKyvLDG-KELEAPISAHQRVGEIE 352

                        330       340       350
                 ....*....|....*....|....*....|
gi 521994452 363 VTLAGVEITRVPLVALEAVAEGGLWERIRD 392
Cdd:PRK11397 353 LYDRDKQVAHWPLVTLESVGEGGMFSRLSD 382
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
53-273 1.03e-91

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 275.80  E-value: 1.03e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452   53 EAKGYLLVDFNTGAVLAESNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAWRTGG---SKMFVEVGKRVG 129
Cdd:pfam00768   7 AAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLKPGSQVS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  130 LEDLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANHYTTARDIAKVTVALIREFPQ 209
Cdd:pfam00768  87 VKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKALIKDLPE 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  210 yyVWDGTKEYEY-----NGIKQHNRNRLLWRDS-TVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGAK 273
Cdd:pfam00768 167 --ELSITKEKSFtfrgiNKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 293-383 3.13e-27

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: 103.45  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452   293 YESHRLYPGGEPVKSLRVWKGDREEVPIGPARDVLATIPRGRYAELSARMD-QAPTLTAPIAQGTRLGDIVVTLAGVEIT 371
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVlDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 521994452   372 RVPLVALEAVAE 383
Cdd:smart00936  81 EVPLVALEDVEK 92
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 58-272 4.82e-25

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 103.61  E-value: 4.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  58 LLVDFNTGAVLAESNADLRLEPASLTKIMTGY-TLyrelaegHAHLT-DQVL---ISENAWRTG-GSKmfVEVGKRVGLE 131
Cdd:PRK11669  45 MVVDLNTNKVIYSSNPDLVVPIASITKLMTAMvVL-------DAKLPlDEKLkvdISQTPEMKGvYSR--VRLNSEISRK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452 132 DLLKGMIIQSGNDASVALAEHVAGSEQVFAELMNAQAQRLGMTNSHFVNVTGLPDANhYTTARDIAKVTVAlIREFPQYY 211
Cdd:PRK11669 116 DMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPTGLSIHN-VSTARDLTKLLIA-SKQYPLIG 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521994452 212 VWDGTKEYEYNGIKQ------HNRNRLLWRDS-TVDGVKTGYTQNAGYCLVASAKRDDMRLVSVVLGA 272
Cdd:PRK11669 194 QLSTTREKTATFRKPnytlpfRNTNHLVYRDNwNIQLTKTGFTNAAGHCLVMRTVINNRPVALVVLDA 261
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 293-383 2.27e-21

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: 87.65  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  293 YESHRLYPGGEPVKSLRVWKGDREEVPIGPARDVLATIPRGRYAELSARMDQAPTLTAPIAQGTRLGDIVVTLAGVEITR 372
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKPLEAPIKKGQVVGKLEVYLDGKLIGE 80

                          90
                  ....*....|.
gi 521994452  373 VPLVALEAVAE 383
Cdd:pfam07943  81 VPLVAKEDVEE 91
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 56-205 4.70e-14

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: 70.77  E-value: 4.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452   56 GYLLVDFNTGAVLAeSNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISENAwRTGGSKMF--VEVGKRVGLEDL 133
Cdd:pfam13354   1 GIYVRDLDTGEELG-INGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAED-KVGGSGILqyLPDGSQLSLRDL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521994452  134 LKGMIIQSGNDASVALAEHVAGSEqvfaelMNAQAQRLGMTNSHFVNvtGLPDANH-------YTTARDIAKVTVALIR 205
Cdd:pfam13354  79 LTLMIAVSDNTATNLLIDRLGLEA------VNARLRALGLRDTRLRR--KLPDLRAadkggtnTTTARDMAKLLEALYR 149
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
56-205 7.20e-12

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 65.30  E-value: 7.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521994452  56 GYLLVDFNTGAVLAEsNADLRLEPASLTKIMTGYTLYRELAEGHAHLTDQVLISEnAWRTGGSKMFVE--VGKRVGLEDL 133
Cdd:COG2367   36 GVYVLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTP-EDLVGGSGILQKlpDGTGLTLREL 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521994452 134 LKGMIIQSGNDASVALAEHVaGSEQVfaelmNAQAQRLGMTNSHFVNVTG-----LPDANHYTTARDIAKVTVALIR 205
Cdd:COG2367  114 AELMITVSDNTATNLLLRLL-GPDAV-----NAFLRSLGLTDTRLDRKEPdlnelPGDGRNTTTPRDMARLLAALYR 184
 
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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