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Conserved domains on  [gi|504696038|ref|WP_014883140|]
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MULTISPECIES: serine-type D-Ala-D-Ala carboxypeptidase [Enterobacter]

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;
1-401 0e+00

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


:

Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 838.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   1 MTRKMTSLRSLAAGSALLFLFAPTLYAAEQAAPEAPpVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 80
Cdd:PRK10001   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPS-VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  81 LKAGKIKLDDMVTIGKDAWATGNPALRGSSVMFLKPGDQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYA 160
Cdd:PRK10001  80 LKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 161 QKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIHDVPDEYAIHKEKEFTFNKIRQPNRNRLLWSSNVNVDGMKTGTT 240
Cdd:PRK10001 160 KKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 241 AGAGYNLVASATQGDMRLISVVLGTKTDRIRFNESEKLLTWGFRFYETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGS 320
Cdd:PRK10001 240 AGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 321 VTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMEAVEEGGFFSRMWDFVLMKFHSWFGSWF 400
Cdd:PRK10001 320 VTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWF 399


                 .
gi 504696038 401 S 401
Cdd:PRK10001 400 S 400
 
Name Accession Description Interval E-value
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
1-401 0e+00

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 838.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   1 MTRKMTSLRSLAAGSALLFLFAPTLYAAEQAAPEAPpVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 80
Cdd:PRK10001   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPS-VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  81 LKAGKIKLDDMVTIGKDAWATGNPALRGSSVMFLKPGDQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYA 160
Cdd:PRK10001  80 LKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 161 QKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIHDVPDEYAIHKEKEFTFNKIRQPNRNRLLWSSNVNVDGMKTGTT 240
Cdd:PRK10001 160 KKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 241 AGAGYNLVASATQGDMRLISVVLGTKTDRIRFNESEKLLTWGFRFYETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGS 320
Cdd:PRK10001 240 AGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 321 VTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMEAVEEGGFFSRMWDFVLMKFHSWFGSWF 400
Cdd:PRK10001 320 VTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWF 399


                 .
gi 504696038 401 S 401
Cdd:PRK10001 400 S 400
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
9-383 1.22e-144

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 413.85  E-value: 1.22e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   9 RSLAAGSALLFLFAPTlyaaeQAAPEAPPVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAGKIKL 88
Cdd:COG1686    2 KKLLLLALLLLLAAAA-----AAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  89 DDMVTIGKDAWATGnpalrgSSVMFLKPGDQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLTNT 168
Cdd:COG1686   77 DDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 169 TFKTVHGLDAPGQFSTARDMALLGKALIHDVPDEYAIHKEKEFTFN---KIRQPNRNRLLWSSNvNVDGMKTGTTAGAGY 245
Cdd:COG1686  151 HFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGYTDAAGY 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 246 NLVASATQGDMRLISVVLGTKTDRIRFNESEKLLTWGFrfyetvtpikpdatfvsqrvwfgdksevnlgageagsvtiPR 325
Cdd:COG1686  230 CLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PK 269

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504696038 326 GQlkNLKASFTLTDPqLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMEAVEEGGFFSR 383
Cdd:COG1686  270 GE--ALKAEVVLDGP-LKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
38-266 3.78e-127

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 365.94  E-value: 3.78e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   38 VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLDDMVTIGKDAWATGNPalrGSSVMFLKPG 117
Cdd:pfam00768   6 IAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNIFLKPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  118 DQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIH 197
Cdd:pfam00768  83 SQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKALIK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696038  198 DVPDEYAIHKEKEFTF---NKIRQPNRNRLLWSSNVNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGTK 266
Cdd:pfam00768 163 DLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 286-377 9.64e-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: 115.78  E-value: 9.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   286 YETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDFQLNGKSIE 365
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 504696038   366 QRPLIVMEAVEE 377
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
1-401 0e+00

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 838.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   1 MTRKMTSLRSLAAGSALLFLFAPTLYAAEQAAPEAPpVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 80
Cdd:PRK10001   1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPS-VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  81 LKAGKIKLDDMVTIGKDAWATGNPALRGSSVMFLKPGDQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYA 160
Cdd:PRK10001  80 LKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 161 QKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIHDVPDEYAIHKEKEFTFNKIRQPNRNRLLWSSNVNVDGMKTGTT 240
Cdd:PRK10001 160 KKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 241 AGAGYNLVASATQGDMRLISVVLGTKTDRIRFNESEKLLTWGFRFYETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGS 320
Cdd:PRK10001 240 AGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 321 VTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMEAVEEGGFFSRMWDFVLMKFHSWFGSWF 400
Cdd:PRK10001 320 VTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWF 399


                 .
gi 504696038 401 S 401
Cdd:PRK10001 400 S 400
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 38-397 0e+00

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 581.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  38 VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLDDMVTIGKDAWATGNPALRGSSVMFLKPG 117
Cdd:PRK10793  44 IDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 118 DQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIH 197
Cdd:PRK10793 124 MQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 198 DVPDEYAIHKEKEFTFNKIRQPNRNRLLWSSNVNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGTKTDRIRFNESEK 277
Cdd:PRK10793 204 DVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKK 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 278 LLTWGFRFYETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDF 357
Cdd:PRK10793 284 LLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINF 363

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 504696038 358 QLNGKSIEQRPLIVMEAVEEGGFFSRMWDFVLMKFHSWFG 397
Cdd:PRK10793 364 QLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG 403
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
38-392 4.48e-160

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 455.43  E-value: 4.48e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  38 VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLDDMVTIGKDAWATGNPALRGSSVMFLKPG 117
Cdd:PRK11397  34 IDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 118 DQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIH 197
Cdd:PRK11397 114 DRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIH 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 198 DVPDEYAIHKEKEFTFNKIRQPNRNRLLWSSNVNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGTKTDRIRFNESEK 277
Cdd:PRK11397 194 GEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARK 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 278 LLTWGFRFYETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDF 357
Cdd:PRK11397 274 LLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVGEIEL 353

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 504696038 358 QLNGKSIEQRPLIVMEAVEEGGFFSRMWDFVLMKF 392
Cdd:PRK11397 354 YDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
9-383 1.22e-144

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 413.85  E-value: 1.22e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   9 RSLAAGSALLFLFAPTlyaaeQAAPEAPPVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAGKIKL 88
Cdd:COG1686    2 KKLLLLALLLLLAAAA-----AAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  89 DDMVTIGKDAWATGnpalrgSSVMFLKPGDQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLTNT 168
Cdd:COG1686   77 DDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 169 TFKTVHGLDAPGQFSTARDMALLGKALIHDVPDEYAIHKEKEFTFN---KIRQPNRNRLLWSSNvNVDGMKTGTTAGAGY 245
Cdd:COG1686  151 HFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGYTDAAGY 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 246 NLVASATQGDMRLISVVLGTKTDRIRFNESEKLLTWGFrfyetvtpikpdatfvsqrvwfgdksevnlgageagsvtiPR 325
Cdd:COG1686  230 CLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PK 269

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504696038 326 GQlkNLKASFTLTDPqLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMEAVEEGGFFSR 383
Cdd:COG1686  270 GE--ALKAEVVLDGP-LKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
38-266 3.78e-127

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 365.94  E-value: 3.78e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   38 VDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLDDMVTIGKDAWATGNPalrGSSVMFLKPG 117
Cdd:pfam00768   6 IAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNIFLKPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  118 DQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLTNTTFKTVHGLDAPGQFSTARDMALLGKALIH 197
Cdd:pfam00768  83 SQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKALIK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504696038  198 DVPDEYAIHKEKEFTF---NKIRQPNRNRLLWSSNVNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGTK 266
Cdd:pfam00768 163 DLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 286-377 9.64e-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: 115.78  E-value: 9.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   286 YETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASFTLTDPQLTAPLKKGQVVGTIDFQLNGKSIE 365
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 504696038   366 QRPLIVMEAVEE 377
Cdd:smart00936  81 EVPLVALEDVEK 92
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 286-377 2.68e-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: 111.92  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  286 YETVTPIKPDATFVSQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASFTLTDPqLTAPLKKGQVVGTIDFQLNGKSIE 365
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-LEAPIKKGQVVGKLEVYLDGKLIG 79

                          90
                  ....*....|..
gi 504696038  366 QRPLIVMEAVEE 377
Cdd:pfam07943  80 EVPLVAKEDVEE 91
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 17-296 5.59e-21

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 92.44  E-value: 5.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  17 LLFLFAPTLYAAEQAAPEAPPVDARAW--------ILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAlkagKIKL 88
Cdd:PRK11669  10 LLLLLAGVPFAPQAVAKTAAATTASQPqeiasgsaMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  89 DDMVTIGkdawATGNPALRG--SSVmflKPGDQVSVSDLNKGVIIQSGNDACIALADYVAGSQDSFIGLMNGYAQKLGLT 166
Cdd:PRK11669  86 DEKLKVD----ISQTPEMKGvySRV---RLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 167 NTTFKTVHGLdAPGQFSTARDMALLGKAlIHDVP--DEYAIHKEKEFTFnkiRQP-------NRNRLLWSSNVNVDGMKT 237
Cdd:PRK11669 159 NTRYVEPTGL-SIHNVSTARDLTKLLIA-SKQYPliGQLSTTREKTATF---RKPnytlpfrNTNHLVYRDNWNIQLTKT 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504696038 238 GTTAGAGYNLVASATQGDMRLISVVLGTKTDRIRFNESEKLLTWgfrfYET--VTPIKPDA 296
Cdd:PRK11669 234 GFTNAAGHCLVMRTVINNRPVALVVLDAFGKYTHFADASRLRTW----IETgkVTPVPAAA 290
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 58-198 2.32e-13

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: 68.84  E-value: 2.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038   58 NADEKLDPASLTKIMTSYVVGQALKAGKIKLDDMVTIGKDAWATGNPALRgssvmFLKPGDQVSVSDLNKGVIIQSGNDA 137
Cdd:pfam13354  16 NGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQ-----YLPDGSQLSLRDLLTLMIAVSDNTA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504696038  138 CIALADYVAGSQdsfiglMNGYAQKLGLTNTTF----KTVHGLDAPGQ-FSTARDMALLGKALIHD 198
Cdd:pfam13354  91 TNLLIDRLGLEA------VNARLRALGLRDTRLrrklPDLRAADKGGTnTTTARDMAKLLEALYRG 150
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
39-195 2.18e-12

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 66.85  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038  39 DARAWI-LMDYASGKVLAEgNADEKLDPASLTKIMTSYVVGQALKAGKIKLDDMVTIGKDAWATGNPALRgssvmFLKPG 117
Cdd:COG2367   32 GGRVGVyVLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGILQ-----KLPDG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696038 118 DQVSVSDLNKGVIIQSGNDACIALADYVAGSQdsfiglMNGYAQKLGLTNTTF--KTVHGLDAPGQF---STARDMALLG 192
Cdd:COG2367  106 TGLTLRELAELMITVSDNTATNLLLRLLGPDA------VNAFLRSLGLTDTRLdrKEPDLNELPGDGrntTTPRDMARLL 179


                 ...
gi 504696038 193 KAL 195
Cdd:COG2367  180 AAL 182
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
51-90 5.34e-03

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


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 38.51  E-value: 5.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504696038  51 GKVLAE---GNAD----EKLDP------ASLTKIMTSYVVGQALKAGKIKLDD 90
Cdd:COG1680   43 GKVVYEkayGVADletgRPVTPdtlfriASVTKSFTATAVLQLVEEGKLDLDD 95
 
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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