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Conserved domains on  [gi|446118106|ref|WP_000195961|]
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MULTISPECIES: serine-type D-Ala-D-Ala carboxypeptidase [Enterobacteriaceae]

Protein Classification

serine-type D-Ala-D-Ala carboxypeptidase( domain architecture ID 11484551)

serine-type D-Ala-D-Ala carboxypeptidase removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
1-400 0e+00

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


:

Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 876.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80
Cdd:PRK10001   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160
Cdd:PRK10001  81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240
Cdd:PRK10001 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRMWDFVMMKFHQWFGSWFS 400
Cdd:PRK10001 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWFS 400
 
Name Accession Description Interval E-value
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
1-400 0e+00

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 876.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80
Cdd:PRK10001   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160
Cdd:PRK10001  81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240
Cdd:PRK10001 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRMWDFVMMKFHQWFGSWFS 400
Cdd:PRK10001 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWFS 400
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
17-382 6.94e-147

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 419.24  E-value: 6.94e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  17 FLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKD 96
Cdd:COG1686    6 LLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  97 AWATGnpalrgSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLD 176
Cdd:COG1686   86 AARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 177 APGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFN---KIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQG 253
Cdd:COG1686  160 DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGYTDAAGYCLVASAKRG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 254 DMRLISVVLGAKTDRIRFNESEKLLTWGFrffetvtpikpdatfvtqrvwfgdksevnlgageagsvtiPRGQlkNLKAS 333
Cdd:COG1686  239 GRRLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKGE--ALKAE 276

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 446118106 334 YTLTEPqLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGR 382
Cdd:COG1686  277 VVLDGP-LKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
32-265 7.19e-132

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 377.88  E-value: 7.19e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   32 VEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPalrGSSVM 111
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  112 FLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLG 191
Cdd:pfam00768  78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446118106  192 KALIHDVPEEYAIHKEKEFTF---NKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAK 265
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 285-376 1.47e-32

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: 117.70  E-value: 1.47e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   285 FETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIE 364
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 446118106   365 QRPLIVMENVEE 376
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
1-400 0e+00

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 876.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80
Cdd:PRK10001   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160
Cdd:PRK10001  81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240
Cdd:PRK10001 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRMWDFVMMKFHQWFGSWFS 400
Cdd:PRK10001 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWFS 400
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 5-396 0e+00

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 591.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   5 SSLLRGLAAGSAFLFLFAPTAFAAEQTVE-----APSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 79
Cdd:PRK10793   7 ARIMKRLALTTALCTAFISAAHADDLNIKtmipgVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  80 LKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYA 159
Cdd:PRK10793  87 MKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 160 KKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTT 239
Cdd:PRK10793 167 NALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHT 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 240 AGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGS 319
Cdd:PRK10793 247 DKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVY 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446118106 320 VTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRMWDFVMMKFHQWFG 396
Cdd:PRK10793 327 LTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG 403
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
9-391 2.50e-165

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 468.92  E-value: 2.50e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   9 RGLAAGSAFLFLFAPtAFAAEQ---TVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKI 85
Cdd:PRK11397   4 RLIIAASLFAFNLSS-AFAAENipfSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  86 KLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLT 165
Cdd:PRK11397  83 TPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 166 NTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYN 245
Cdd:PRK11397 163 DTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFN 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 246 LVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRG 325
Cdd:PRK11397 243 LIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKA 322

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446118106 326 QLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGRMWDFVMMKF 391
Cdd:PRK11397 323 EIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
17-382 6.94e-147

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 419.24  E-value: 6.94e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  17 FLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKD 96
Cdd:COG1686    6 LLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  97 AWATGnpalrgSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLD 176
Cdd:COG1686   86 AARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 177 APGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFN---KIRQPNRNRLLWSSNlNVDGMKTGTTAGAGYNLVASATQG 253
Cdd:COG1686  160 DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGYTDAAGYCLVASAKRG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 254 DMRLISVVLGAKTDRIRFNESEKLLTWGFrffetvtpikpdatfvtqrvwfgdksevnlgageagsvtiPRGQlkNLKAS 333
Cdd:COG1686  239 GRRLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKGE--ALKAE 276

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 446118106 334 YTLTEPqLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFGR 382
Cdd:COG1686  277 VVLDGP-LKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
32-265 7.19e-132

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 377.88  E-value: 7.19e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   32 VEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPalrGSSVM 111
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  112 FLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLG 191
Cdd:pfam00768  78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446118106  192 KALIHDVPEEYAIHKEKEFTF---NKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAK 265
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 285-376 1.47e-32

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: 117.70  E-value: 1.47e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   285 FETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIE 364
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 446118106   365 QRPLIVMENVEE 376
Cdd:smart00936  81 EVPLVALEDVEK 92
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 285-376 1.12e-30

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: 112.69  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  285 FETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPqLTAPLKKGQVVGTIDFQLNGKSIE 364
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-LEAPIKKGQVVGKLEVYLDGKLIG 79

                          90
                  ....*....|..
gi 446118106  365 QRPLIVMENVEE 376
Cdd:pfam07943  80 EVPLVAKEDVEE 91
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 20-295 2.39e-23

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 98.98  E-value: 2.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  20 LFAPTAFAAEQTVEAPS----VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAlkadKIKLTDMVTVGk 95
Cdd:PRK11669  18 PFAPQAVAKTAAATTASqpqeIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPLDEKLKVD- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  96 dawATGNPALRG--SSVmflKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVH 173
Cdd:PRK11669  93 ---ISQTPEMKGvySRV---RLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106 174 GLdAPGQFSTARDMALLGKAlIHDVP--EEYAIHKEKEFTFnkiRQP-------NRNRLLWSSNLNVDGMKTGTTAGAGY 244
Cdd:PRK11669 167 GL-SIHNVSTARDLTKLLIA-SKQYPliGQLSTTREKTATF---RKPnytlpfrNTNHLVYRDNWNIQLTKTGFTNAAGH 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446118106 245 NLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWgfrfFET--VTPIKPDA 295
Cdd:PRK11669 242 CLVMRTVINNRPVALVVLDAFGKYTHFADASRLRTW----IETgkVTPVPAAA 290
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 57-197 2.66e-12

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: 65.76  E-value: 2.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106   57 NADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRgssvmFLKPGDQVSVADLNKGVIIQSGNDA 136
Cdd:pfam13354  16 NGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQ-----YLPDGSQLSLRDLLTLMIAVSDNTA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446118106  137 CIALADYVAGSQesfiglMNGYAKKLGLTNTTFQ----TVHGLDAPGQ-FSTARDMALLGKALIHD 197
Cdd:pfam13354  91 TNLLIDRLGLEA------VNARLRALGLRDTRLRrklpDLRAADKGGTnTTTARDMAKLLEALYRG 150
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
16-194 3.72e-12

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 66.07  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  16 AFLFLFAPTAFAAEQTVEAP------SVDARAWI-LMDYASGKVLAEgNADEKLDPASLTKIMTSYVVGQALKADKIKLT 88
Cdd:COG2367    4 LALLLLAAAAAAPASALEAElaaleaALGGRVGVyVLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118106  89 DMVTVGKDAWATGNPALRgssvmFLKPGDQVSVADLNKGVIIQSGNDACIALADYVaGSQEsfiglMNGYAKKLGLTNTT 168
Cdd:COG2367   83 ERVTLTPEDLVGGSGILQ-----KLPDGTGLTLRELAELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTR 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446118106 169 FQ-TVHGL-DAPGQF---STARDMALLGKAL 194
Cdd:COG2367  152 LDrKEPDLnELPGDGrntTTPRDMARLLAAL 182
 
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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