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Conserved domains on  [gi|1523361225|gb|RQL43539|]
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D-alanyl-D-alanine carboxypeptidase [Neisseria meningitidis]

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];
5-381 1.25e-114

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


:

Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 336.81  E-value: 1.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225   5 KILPVLLSIILGVSHATAASPAPNKPAVHAaptfqtpetltaahIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFK 84
Cdd:COG1686     2 KKLLLLALLLLLAAAAAAPAAPPDIAAKSA--------------ILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  85 NMKSGNIRSEENLKIPESAWASEGSRMFVRPGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLG 164
Cdd:COG1686    68 ALKAGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIA-GSEEAFVALMNAKAKELG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 165 MKNTVFKNPTGLSREGQVSTAKDLAQLSEALMRDFPEYYPLFSIKSFKFKN---IEQNNRNILLYRDNNVNGLKAGHTES 241
Cdd:COG1686   147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNgrgITLRNTNRLLGRYPGVDGLKTGYTDA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 242 GGYNLAVSYSGNGRHILVITLGSESAETRASDNSKLLNWAlqafdtpkiYPKGKTVaqiqisggskktvragflkEAYIT 321
Cdd:COG1686   227 AGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG---------FPKGEAL-------------------KAEVV 278

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 322 LPhkeakmaeqiletiQPIPAPVKKGQILGKIKIRQNGYTIAEKEIVALENVEKRSRWQR 381
Cdd:COG1686   279 LD--------------GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
5-381 1.25e-114

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 336.81  E-value: 1.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225   5 KILPVLLSIILGVSHATAASPAPNKPAVHAaptfqtpetltaahIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFK 84
Cdd:COG1686     2 KKLLLLALLLLLAAAAAAPAAPPDIAAKSA--------------ILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  85 NMKSGNIRSEENLKIPESAWASEGSRMFVRPGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLG 164
Cdd:COG1686    68 ALKAGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIA-GSEEAFVALMNAKAKELG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 165 MKNTVFKNPTGLSREGQVSTAKDLAQLSEALMRDFPEYYPLFSIKSFKFKN---IEQNNRNILLYRDNNVNGLKAGHTES 241
Cdd:COG1686   147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNgrgITLRNTNRLLGRYPGVDGLKTGYTDA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 242 GGYNLAVSYSGNGRHILVITLGSESAETRASDNSKLLNWAlqafdtpkiYPKGKTVaqiqisggskktvragflkEAYIT 321
Cdd:COG1686   227 AGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG---------FPKGEAL-------------------KAEVV 278

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 322 LPhkeakmaeqiletiQPIPAPVKKGQILGKIKIRQNGYTIAEKEIVALENVEKRSRWQR 381
Cdd:COG1686   279 LD--------------GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
30-383 3.73e-77

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 243.75  E-value: 3.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  30 PAVHAA-PTFQTPETLTAAHIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESAWAS-- 106
Cdd:PRK10001   23 PTAFAAeQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATgn 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 107 ---EGSR-MFVRPGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLGMKNTVFKNPTGLSREGQV 182
Cdd:PRK10001  103 palRGSSvMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVA-GSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 183 STAKDLAQLSEALMRDFPEYYPLFSIKSFKFKNIEQNNRNILLYRDN-NVNGLKAGHTESGGYNLAVSYSGNGRHILVIT 261
Cdd:PRK10001  182 STARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQGDMRLISVV 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 262 LGSESAETRASDNSKLLNWALQAFDT-PKIYPKGKTVAQiQISGGSKKTVRAGFLKEAYITLPHKEAKMAEQILETIQP- 339
Cdd:PRK10001  262 LGAKTDRIRFNESEKLLTWGFRFFETvTPIKPDATFVTQ-RVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPq 340

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1523361225 340 IPAPVKKGQILGKIKIRQNGYTIAEKEIVALENVEKRSRWQRLW 383
Cdd:PRK10001  341 LTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMW 384
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
40-263 2.33e-61

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 197.61  E-value: 2.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  40 TPETLTAAH-IVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESAWASEG---SRMFVRP 115
Cdd:pfam00768   2 SAPEIAAKSaILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 116 GDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLGMKNTVFKNPTGLSREGQVSTAKDLAQLSEAL 195
Cdd:pfam00768  82 GSQVSVKDLLRGALVSSGNDAAVALAEHIA-GSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1523361225 196 MRDFPEYYPLFSIKSFKF---KNIEQNNRNILLYRDN-NVNGLKAGHTESGGYNLAVSYSGNGRHILVITLG 263
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMG 232
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 285-375 5.23e-22

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: 89.20  E-value: 5.23e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  285 FDTPKIYPKGKTVAQIQISGGSKKTVRAGFLKEAYITLPHKEAKMAEQILETIQP-IPAPVKKGQILGKIKIRQNGYTIA 363
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPeLEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 1523361225  364 EKEIVALENVEK 375
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
5-381 1.25e-114

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 336.81  E-value: 1.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225   5 KILPVLLSIILGVSHATAASPAPNKPAVHAaptfqtpetltaahIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFK 84
Cdd:COG1686     2 KKLLLLALLLLLAAAAAAPAAPPDIAAKSA--------------ILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  85 NMKSGNIRSEENLKIPESAWASEGSRMFVRPGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLG 164
Cdd:COG1686    68 ALKAGKISLDDKVTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIA-GSEEAFVALMNAKAKELG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 165 MKNTVFKNPTGLSREGQVSTAKDLAQLSEALMRDFPEYYPLFSIKSFKFKN---IEQNNRNILLYRDNNVNGLKAGHTES 241
Cdd:COG1686   147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNgrgITLRNTNRLLGRYPGVDGLKTGYTDA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 242 GGYNLAVSYSGNGRHILVITLGSESAETRASDNSKLLNWAlqafdtpkiYPKGKTVaqiqisggskktvragflkEAYIT 321
Cdd:COG1686   227 AGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG---------FPKGEAL-------------------KAEVV 278

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 322 LPhkeakmaeqiletiQPIPAPVKKGQILGKIKIRQNGYTIAEKEIVALENVEKRSRWQR 381
Cdd:COG1686   279 LD--------------GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
30-383 3.73e-77

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 243.75  E-value: 3.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  30 PAVHAA-PTFQTPETLTAAHIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESAWAS-- 106
Cdd:PRK10001   23 PTAFAAeQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATgn 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 107 ---EGSR-MFVRPGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLGMKNTVFKNPTGLSREGQV 182
Cdd:PRK10001  103 palRGSSvMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVA-GSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 183 STAKDLAQLSEALMRDFPEYYPLFSIKSFKFKNIEQNNRNILLYRDN-NVNGLKAGHTESGGYNLAVSYSGNGRHILVIT 261
Cdd:PRK10001  182 STARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQGDMRLISVV 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 262 LGSESAETRASDNSKLLNWALQAFDT-PKIYPKGKTVAQiQISGGSKKTVRAGFLKEAYITLPHKEAKMAEQILETIQP- 339
Cdd:PRK10001  262 LGAKTDRIRFNESEKLLTWGFRFFETvTPIKPDATFVTQ-RVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPq 340

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1523361225 340 IPAPVKKGQILGKIKIRQNGYTIAEKEIVALENVEKRSRWQRLW 383
Cdd:PRK10001  341 LTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMW 384
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
13-382 2.62e-75

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 238.57  E-value: 2.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  13 IILGVSHATAASPAPNKPavhaaptfQTPETLTAAHIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFKNMKSGNIR 92
Cdd:PRK11397   12 FAFNLSSAFAAENIPFSP--------QPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRIT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  93 SEENLKIPESAWAS-----EGSR-MFVRPGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLGMK 166
Cdd:PRK11397   84 PDDIVTVGRDAWAKdnpvfVGSSlMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIA-GGQRQFVEMMNNYVEKLHLK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 167 NTVFKNPTGLSREGQVSTAKDLAQLSEALMRDFPEYYPLFSIKSFKFKNIEQNNRNILLYRDN-NVNGLKAGHTESGGYN 245
Cdd:PRK11397  163 DTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTmNVDGLKTGHTSGAGFN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 246 LAVSYSGNGRHILVITLGSESAETRASDNSKLLNWALQAFDTPKIYPKGKTVAQIQISGGSKKTVRAGFLKEAYITLPHK 325
Cdd:PRK11397  243 LIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKA 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1523361225 326 EAK--MAEQILETiQPIPAPVKKGQILGKIKIRQNGYTIAEKEIVALENVEKRSRWQRL 382
Cdd:PRK11397  323 EIPhiKAKYVLDG-KELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRL 380
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 41-382 9.26e-71

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 227.43  E-value: 9.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  41 PETLTAAHIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESAWAS-----EGSR-MFVR 114
Cdd:PRK10793   42 PQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATgnpvfKGSSlMFLK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 115 PGDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLGMKNTVFKNPTGLSREGQVSTAKDLAQLSEA 194
Cdd:PRK10793  122 PGMQVPVSQLIRGINLQSGNDACVAMADYVA-GSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 195 LMRDFPEYYPLFSIKSFKFKNIEQNNRNILLYRDN-NVNGLKAGHTESGGYNLAVSYS-GNGRHILVItLGSESAETRAS 272
Cdd:PRK10793  201 LIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSlNVDGIKTGHTDKAGYNLVASATeGQMRLISAV-MGGRTFKGRET 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 273 DNSKLLNWALQAFDTPKIYPKGKTVAQIQISGGSKKTVRAGFLKEAYITLPHKEAK--MAEQILETIQpIPAPVKKGQIL 350
Cdd:PRK10793  280 ESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKdlKASYVLNTSE-LHAPLQKNQVV 358

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1523361225 351 GKIKIRQNGYTIAEKEIVALENVEKRSRWQRL 382
Cdd:PRK10793  359 GTINFQLDGKTIEQRPLVVLQEIPEGNFFGKI 390
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
40-263 2.33e-61

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 197.61  E-value: 2.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  40 TPETLTAAH-IVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESAWASEG---SRMFVRP 115
Cdd:pfam00768   2 SAPEIAAKSaILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 116 GDTVSTDKLLKGMIALSANDAALTLAGRLGnGSIENFVQQMNKEARRLGMKNTVFKNPTGLSREGQVSTAKDLAQLSEAL 195
Cdd:pfam00768  82 GSQVSVKDLLRGALVSSGNDAAVALAEHIA-GSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1523361225 196 MRDFPEYYPLFSIKSFKF---KNIEQNNRNILLYRDN-NVNGLKAGHTESGGYNLAVSYSGNGRHILVITLG 263
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMG 232
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 5-280 7.88e-24

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 100.14  E-value: 7.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225   5 KILPVLLSIILGVSHATAASPAPNKPAVhAAPTFQTPETLTAAHIVIDLQSKQILSAKNINTPVEPAALTQLMTAYLVFk 84
Cdd:PRK11669    2 KFRVSLLSLLLLLAGVPFAPQAVAKTAA-ATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  85 nmkSGNIRSEENLKI-----PESawasEG--SRmfVRPGDTVSTDKLLkgMIAL--SANDAALTLAGRLgNGSIENFVQQ 155
Cdd:PRK11669   80 ---DAKLPLDEKLKVdisqtPEM----KGvySR--VRLNSEISRKDML--LLALmsSENRAAASLAHHY-PGGYKAFIKA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 156 MNKEARRLGMKNTVFKNPTGLSREgQVSTAKDLAQLSEAlmrdfPEYYPLFSI------KSFKFKN----IEQNNRNILL 225
Cdd:PRK11669  148 MNAKAKALGMTNTRYVEPTGLSIH-NVSTARDLTKLLIA-----SKQYPLIGQlsttreKTATFRKpnytLPFRNTNHLV 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1523361225 226 YRDN-NVNGLKAGHTESGGYNLAVSYSGNGRHILVITLGSESAETRASDNSKLLNW 280
Cdd:PRK11669  222 YRDNwNIQLTKTGFTNAAGHCLVMRTVINNRPVALVVLDAFGKYTHFADASRLRTW 277
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 285-375 5.23e-22

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: 89.20  E-value: 5.23e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  285 FDTPKIYPKGKTVAQIQISGGSKKTVRAGFLKEAYITLPHKEAKMAEQILETIQP-IPAPVKKGQILGKIKIRQNGYTIA 363
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPeLEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 1523361225  364 EKEIVALENVEK 375
Cdd:smart00936  81 EVPLVALEDVEK 92
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 285-375 1.34e-18

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: 79.95  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225 285 FDTPKIYPKGKTVAQIQISGGSKKTVRAGFLKEAYITLPHKEAKMAEQILETIQPIPAPVKKGQILGKIKIRQNGYTIAE 364
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKPLEAPIKKGQVVGKLEVYLDGKLIGE 80

                          90
                  ....*....|.
gi 1523361225 365 KEIVALENVEK 375
Cdd:pfam07943  81 VPLVAKEDVEE 91
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 50-195 1.76e-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: 60.37  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  50 VIDLQSKQILSaKNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESAwASEGSRMF--VRPGDTVSTDKLLKG 127
Cdd:pfam13354   4 VRDLDTGEELG-INGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAED-KVGGSGILqyLPDGSQLSLRDLLTL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1523361225 128 MIALSANDAALTLAGRLGNGSIenfvqqmNKEARRLGMKNTVFKNPTGLSREGQ-----VSTAKDLAQLSEAL 195
Cdd:pfam13354  82 MIAVSDNTATNLLIDRLGLEAV-------NARLRALGLRDTRLRRKLPDLRAADkggtnTTTARDMAKLLEAL 147
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
50-198 5.06e-06

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 47.59  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361225  50 VIDLQSKQILSAkNINTPVEPAALTQLMTAYLVFKNMKSGNIRSEENLKIPESaWASEGS--RMFVRPGDTVSTDKLLKG 127
Cdd:COG2367    39 VLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPE-DLVGGSgiLQKLPDGTGLTLRELAEL 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1523361225 128 MIALSANDAALTLAGRLGngsienfVQQMNKEARRLGMKNTVFKN--PTGLSREGQ---VSTAKDLAQLSEALMRD 198
Cdd:COG2367   117 MITVSDNTATNLLLRLLG-------PDAVNAFLRSLGLTDTRLDRkePDLNELPGDgrnTTTPRDMARLLAALYRG 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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