|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-403 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 819.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 1 MKRKVASQTLKYAVAGGLLAVALTGAARADDVNLKTMIPGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTS 80
Cdd:PRK10793 1 MKTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 81 YVIGQAMRAGKFGENDVVTVGKDAWATGNPVFQGSSLMFLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVG 160
Cdd:PRK10793 81 YVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 161 LMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIGQALIRDVPHEYAIYKEKEFTYNNIRQTNRNGLLWDTSMNVDG 240
Cdd:PRK10793 161 LMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 241 IKTGHTASAGYNLVASATEGNMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVSPLKAGREFASEPVWFGDTDRAQLG 320
Cdd:PRK10793 241 IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 321 VDKDVYLTIPRGRMKDLKASYVLNSNELDAPLAKDQVVGTINFQLDGKTIEQRPLVVLNEVKEGGFFSRMIDHIKLLFHR 400
Cdd:PRK10793 321 VDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHH 400
|
...
gi 502612502 401 WFG 403
Cdd:PRK10793 401 WFG 403
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-389 |
2.87e-136 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 392.66 E-value: 2.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 1 MKRKVasqtlkyavaggLLAVALTGAARAddvnlkTMIPGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTS 80
Cdd:COG1686 1 MKKLL------------LLALLLLLAAAA------AAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 81 YVIGQAMRAGKFGENDVVTVGKDAWATGnpvfqgSSLMFLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVG 160
Cdd:COG1686 63 YVVLEALKAGKISLDDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 161 LMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIGQALIRDVPHEYAIYKEKEFTYNN---IRQTNRNGLLWDTSmN 237
Cdd:COG1686 137 LMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNgrgITLRNTNRLLGRYP-G 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 238 VDGIKTGHTASAGYNLVASATEGNMRLISAVMGGRTFKGRETESKKLLTWGFrffetvsplkagrefasepvwfgdtdra 317
Cdd:COG1686 216 VDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF---------------------------- 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612502 318 qlgvdkdvyltiPRGRmkDLKASYVLNsNELDAPLAKDQVVGTINFQLDGKTIEQRPLVVLNEVKEGGFFSR 389
Cdd:COG1686 268 ------------PKGE--ALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
39-272 |
1.20e-120 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 349.38 E-value: 1.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 39 PGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTSYVIGQAMRAGKFGENDVVTVGKDAWATGNPvfqGSSLM 118
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 119 FLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVGLMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIG 198
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612502 199 QALIRDVPHEYAIYKEKEFTY---NNIRQTNRNGLLWDTSMNVDGIKTGHTASAGYNLVASATEGNMRLISAVMGGR 272
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
292-383 |
3.51e-31 |
|
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: 114.24 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 292 FETVSPLKAGREFASEPVWFGDTDRAQLGVDKDVYLTIPRGRMKDLKASYVLNSNELDAPLAKDQVVGTINFQLDGKTIE 371
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 502612502 372 QRPLVVLNEVKE 383
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
43-275 |
1.67e-27 |
|
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.
Pssm-ID: 468436 [Multi-domain] Cd Length: 365 Bit Score: 111.99 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 43 QIDAEAYILIDYNsGKVLAEHNADERRNPASLTKMMTSYVIGQAMRAGKFGENDVVTV-GKDAWATGNPvfqGSSLMFLK 121
Cdd:NF038258 37 QYNPEGAIVTTQT-GQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKItSDYEKMSTLP---NLSTFPLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 122 PGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVGLMNSYVKALGLQNTHFETVHGLDAS--GQF----------- 188
Cdd:NF038258 113 PGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNllKPYapkkykdetks 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 189 -SSARDMALIGQALIRDVPHEYAIYKEKEFTYNNIRQTNRNGLLWDTSM---NVDGIKTGhTASAGYNLVASATEGNMRL 264
Cdd:NF038258 193 kSTAKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRI 271
|
250
....*....|.
gi 502612502 265 ISAVMGGRTFK 275
Cdd:NF038258 272 NQVIMNVGPYP 282
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-403 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 819.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 1 MKRKVASQTLKYAVAGGLLAVALTGAARADDVNLKTMIPGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTS 80
Cdd:PRK10793 1 MKTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 81 YVIGQAMRAGKFGENDVVTVGKDAWATGNPVFQGSSLMFLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVG 160
Cdd:PRK10793 81 YVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 161 LMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIGQALIRDVPHEYAIYKEKEFTYNNIRQTNRNGLLWDTSMNVDG 240
Cdd:PRK10793 161 LMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 241 IKTGHTASAGYNLVASATEGNMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVSPLKAGREFASEPVWFGDTDRAQLG 320
Cdd:PRK10793 241 IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 321 VDKDVYLTIPRGRMKDLKASYVLNSNELDAPLAKDQVVGTINFQLDGKTIEQRPLVVLNEVKEGGFFSRMIDHIKLLFHR 400
Cdd:PRK10793 321 VDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHH 400
|
...
gi 502612502 401 WFG 403
Cdd:PRK10793 401 WFG 403
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
7-403 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 576.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 7 SQTLKYAVAGGLLAVALTGAARADDvnlktMIPGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTSYVIGQA 86
Cdd:PRK10001 5 SSLLRGLAAGSAFLFLFAPTAFAAE-----QTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 87 MRAGKFGENDVVTVGKDAWATGNPVFQGSSLMFLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVGLMNSYV 166
Cdd:PRK10001 80 LKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 167 KALGLQNTHFETVHGLDASGQFSSARDMALIGQALIRDVPHEYAIYKEKEFTYNNIRQTNRNGLLWDTSMNVDGIKTGHT 246
Cdd:PRK10001 160 KKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 247 ASAGYNLVASATEGNMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVSPLKAGREFASEPVWFGDTDRAQLGVDKDVY 326
Cdd:PRK10001 240 AGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGS 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612502 327 LTIPRGRMKDLKASYVLNSNELDAPLAKDQVVGTINFQLDGKTIEQRPLVVLNEVKEGGFFSRMIDHIKLLFHRWFG 403
Cdd:PRK10001 320 VTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFG 396
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
1-396 |
1.46e-180 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 507.44 E-value: 1.46e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 1 MKRKVAsqtlkyaVAGGLLAVALTGAARADDVNLKtmiPGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTS 80
Cdd:PRK11397 1 LKRRLI-------IAASLFAFNLSSAFAAENIPFS---PQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 81 YVIGQAMRAGKFGENDVVTVGKDAWATGNPVFQGSSLMFLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVG 160
Cdd:PRK11397 71 YVVDRAIDSHRITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 161 LMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIGQALIRDVPHEYAIYKEKEFTYNNIRQTNRNGLLWDTSMNVDG 240
Cdd:PRK11397 151 MMNNYVEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 241 IKTGHTASAGYNLVASATEGNMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVSPLKAGREFASEPVWFGDTDRAQLG 320
Cdd:PRK11397 231 LKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALG 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612502 321 VDKDVYLTIPRGRMKDLKASYVLNSNELDAPLAKDQVVGTINFQLDGKTIEQRPLVVLNEVKEGGFFSRMIDHIKL 396
Cdd:PRK11397 311 TEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHH 386
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-389 |
2.87e-136 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 392.66 E-value: 2.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 1 MKRKVasqtlkyavaggLLAVALTGAARAddvnlkTMIPGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTS 80
Cdd:COG1686 1 MKKLL------------LLALLLLLAAAA------AAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 81 YVIGQAMRAGKFGENDVVTVGKDAWATGnpvfqgSSLMFLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVG 160
Cdd:COG1686 63 YVVLEALKAGKISLDDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 161 LMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIGQALIRDVPHEYAIYKEKEFTYNN---IRQTNRNGLLWDTSmN 237
Cdd:COG1686 137 LMNAKAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNgrgITLRNTNRLLGRYP-G 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 238 VDGIKTGHTASAGYNLVASATEGNMRLISAVMGGRTFKGRETESKKLLTWGFrffetvsplkagrefasepvwfgdtdra 317
Cdd:COG1686 216 VDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF---------------------------- 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612502 318 qlgvdkdvyltiPRGRmkDLKASYVLNsNELDAPLAKDQVVGTINFQLDGKTIEQRPLVVLNEVKEGGFFSR 389
Cdd:COG1686 268 ------------PKGE--ALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
39-272 |
1.20e-120 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 349.38 E-value: 1.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 39 PGVPQIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTSYVIGQAMRAGKFGENDVVTVGKDAWATGNPvfqGSSLM 118
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 119 FLKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVGLMNSYVKALGLQNTHFETVHGLDASGQFSSARDMALIG 198
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612502 199 QALIRDVPHEYAIYKEKEFTY---NNIRQTNRNGLLWDTSMNVDGIKTGHTASAGYNLVASATEGNMRLISAVMGGR 272
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
292-383 |
3.51e-31 |
|
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: 114.24 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 292 FETVSPLKAGREFASEPVWFGDTDRAQLGVDKDVYLTIPRGRMKDLKASYVLNSNELDAPLAKDQVVGTINFQLDGKTIE 371
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 502612502 372 QRPLVVLNEVKE 383
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
292-383 |
6.06e-31 |
|
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: 113.46 E-value: 6.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 292 FETVSPLKAGREFASEPVWFGDTDRAQLGVDKDVYLTIPRGRMKDLKASYVLNSNeLDAPLAKDQVVGTINFQLDGKTIE 371
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-LEAPIKKGQVVGKLEVYLDGKLIG 79
|
90
....*....|..
gi 502612502 372 QRPLVVLNEVKE 383
Cdd:pfam07943 80 EVPLVAKEDVEE 91
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
43-275 |
1.67e-27 |
|
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.
Pssm-ID: 468436 [Multi-domain] Cd Length: 365 Bit Score: 111.99 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 43 QIDAEAYILIDYNsGKVLAEHNADERRNPASLTKMMTSYVIGQAMRAGKFGENDVVTV-GKDAWATGNPvfqGSSLMFLK 121
Cdd:NF038258 37 QYNPEGAIVTTQT-GQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKItSDYEKMSTLP---NLSTFPLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 122 PGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVGLMNSYVKALGLQNTHFETVHGLDAS--GQF----------- 188
Cdd:NF038258 113 PGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNllKPYapkkykdetks 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 189 -SSARDMALIGQALIRDVPHEYAIYKEKEFTYNNIRQTNRNGLLWDTSM---NVDGIKTGhTASAGYNLVASATEGNMRL 264
Cdd:NF038258 193 kSTAKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRI 271
|
250
....*....|.
gi 502612502 265 ISAVMGGRTFK 275
Cdd:NF038258 272 NQVIMNVGPYP 282
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
19-272 |
1.12e-13 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 71.25 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 19 LAVALTGAARADDVNLKTMIPGVP----QIDAEAYILIDYNSGKVLAEHNADERRNPASLTKMMTSYVIGQAmragKFGE 94
Cdd:PRK11669 10 LLLLLAGVPFAPQAVAKTAAATTAsqpqEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 95 NDVVTVGkdawATGNPVFQGsslMF--LKPGDQVSVGNLIRGINLVSGNDACVAMADYVAGSQDAFVGLMNSYVKALGLQ 172
Cdd:PRK11669 86 DEKLKVD----ISQTPEMKG---VYsrVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 173 NTHFETVHGLDASgQFSSARDMALIGQAlIRDVP--HEYAIYKEKEFTYNNIRQT----NRNGLLWDTSMNVDGIKTGHT 246
Cdd:PRK11669 159 NTRYVEPTGLSIH-NVSTARDLTKLLIA-SKQYPliGQLSTTREKTATFRKPNYTlpfrNTNHLVYRDNWNIQLTKTGFT 236
|
250 260
....*....|....*....|....*.
gi 502612502 247 ASAGYNLVasategnMRlisAVMGGR 272
Cdd:PRK11669 237 NAAGHCLV-------MR---TVINNR 252
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
61-231 |
4.34e-08 |
|
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: 53.43 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 61 AEHNADERRNPASLTKMMTSYVIGQAMRAGKFGENDVVTVGKDAWATGNPVFQgsslmFLKPGDQVSVGNLIRGINLVSG 140
Cdd:pfam13354 13 LGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQ-----YLPDGSQLSLRDLLTLMIAVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 141 NDACVAMADYVagSQDAFvglmNSYVKALGLQNTHFE----TVHGLDASGQ-FSSARDMALIGQALIRDvphEYAIYKEK 215
Cdd:pfam13354 88 NTATNLLIDRL--GLEAV----NARLRALGLRDTRLRrklpDLRAADKGGTnTTTARDMAKLLEALYRG---ELLSPEST 158
|
170
....*....|....*.
gi 502612502 216 EFTYNNIRQTNRNGLL 231
Cdd:pfam13354 159 DRLLDILSRQQFRDRL 174
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
51-204 |
1.54e-07 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 52.21 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612502 51 LIDYNSGKVLAeHNADERRNPASLTKMMTSYVIGQAMRAGKFGENDVVTVGKDAWATGNPVFQgsslmFLKPGDQVSVGN 130
Cdd:COG2367 39 VLDLDTGETVG-INADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGILQ-----KLPDGTGLTLRE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502612502 131 LIRGINLVSGNDACVAMADYVAGsqDAFvglmNSYVKALGLQNTHF----ETVHGLDASGQ-FSSARDMALIGQALIRD 204
Cdd:COG2367 113 LAELMITVSDNTATNLLLRLLGP--DAV----NAFLRSLGLTDTRLdrkePDLNELPGDGRnTTTPRDMARLLAALYRG 185
|
|
| |
