|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
10-415 |
1.21e-109 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 326.41 E-value: 1.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 10 MVSILALALIVTAFTPmskAKAAEDPFNVNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWD 89
Cdd:COG1686 1 MKKLLLLALLLLLAAA---AAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 90 QTYTPDDYVYEISqdrsLSNVPLRKDGSYTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKELGLTNYKFV 169
Cdd:COG1686 78 DKVTVSEEAARTG----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 170 NATGLenkdlhgkqpkgtgTDEESEVSAKDMALLAQHLIKDHPEILETSSIAKTKFREGtdDEMDMPNWNfmlkGLVKEY 249
Cdd:COG1686 154 NPTGL--------------PDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTN----RLLGRY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 250 EGVDGLKTGSTDSAGSSFTGTAKQGDMRVIAVILNAKGnlHTARFDVAKKLFDYAFknftmkemyKKGQQIkghenievd 329
Cdd:COG1686 214 PGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGF---------PKGEAL--------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 330 kgkdkevpvvtkeafsvpvkngdeksfKAKVNIEKtKLEAPIKKGTKVGMLTTSYSGdekdygylnKDQSGVELITKTGD 409
Cdd:COG1686 274 ---------------------------KAEVVLDG-PLKAPVKKGQVVGTLVVTLDG---------KTIAEVPLVAAEDV 316
|
....*.
gi 500857552 410 EKANWF 415
Cdd:COG1686 317 EKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
38-286 |
2.67e-82 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 253.08 E-value: 2.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 38 VNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWDQTYTPDDYVYEISQDRSlSNVPLRKDGS 117
Cdd:pfam00768 6 IAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLKPGSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 118 YTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKELGLTNYKFVNATGLENKDLHGkqpkgtgtdeesevSA 197
Cdd:pfam00768 85 VSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYS--------------SA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 198 KDMALLAQHLIKDHPEILETSSIAKTKFREgtddemdMPNWNFMLKGLVKEYEG--VDGLKTGSTDSAGSSFTGTAKQGD 275
Cdd:pfam00768 151 RDMAILAKALIKDLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASATKGG 223
|
250
....*....|.
gi 500857552 276 MRVIAVILNAK 286
Cdd:pfam00768 224 MRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
10-322 |
3.56e-70 |
|
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: 226.40 E-value: 3.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 10 MVSILALALIVTAF------TPMSKAKAAEDPF---NVNAKAAILIeASTGKILYSKNAEQRLPIASMAKMMTEYLLLEA 80
Cdd:NF038258 1 IVSLLLLSTIITPPasaaaeTPVEIANQEGYQNlseQYNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 81 IAEGKVKWDQTYTPDDYVYEISQDRSLSNVPLRKDGSYTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKE 160
Cdd:NF038258 80 IKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 161 LGLTNYKFVNATGLENKDLHGKQPKGTGTDEESEVSAKDMALLAQHLIKDHPEILETssiakTKFREGTDDEMDMPNWNF 240
Cdd:NF038258 160 LGMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKY-----TKLTADTQHGVTLYTTNL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 241 MLKGLVKEYEGVDGLKTGSTDSaGSSFTGTAKQGDMRVIAVILNAK--GNLHT--ARFDVAKKLFDYAFKNFTMKEMYKK 316
Cdd:NF038258 235 SLPGQPMSLKGTDGLKTGTSDE-GYNLALTTKRDGLRINQVIMNVGpyPSEGAkhARNKIANALMERAFKQYEYKKVLSK 313
|
....*..
gi 500857552 317 G-QQIKG 322
Cdd:NF038258 314 GeHKIDG 320
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
17-441 |
1.58e-50 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 175.95 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 17 ALIVTAFTPMSKAKAAEDPFNVNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWDQTYT--P 94
Cdd:PRK10001 16 AFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTvgK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 95 DDYVYEISQDRSLSNVPLRKDGSYTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKELGLTNYKFvnatgl 174
Cdd:PRK10001 96 DAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 175 enKDLHGKQPKGTGTdeesevSAKDMALLAQHLIKDHPEiletsSIAKTKFREGTDDEMDMPNWNFMlkgLVKEYEGVDG 254
Cdd:PRK10001 170 --QTVHGLDAPGQFS------TARDMALLGKALIHDVPE-----EYAIHKEKEFTFNKIRQPNRNRL---LWSSNLNVDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 255 LKTGSTDSAGSSFTGTAKQGDMRVIAVILNAKGNlhTARFDVAKKLFDYAFKNFTMKEMYKKGQQIKgheNIEVDKGKDK 334
Cdd:PRK10001 234 MKTGTTAGAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGFRFFETVTPIKPDATFV---TQRVWFGDKS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 335 EVPVVTKEAFSVPVKNGDEKSFKAKVNIEKTKLEAPIKKGTKVGMLTTSYSGdekdygylnkdqsgvelitKTGDEKAnw 414
Cdd:PRK10001 309 EVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNG-------------------KSIEQRP-- 367
|
410 420
....*....|....*....|....*....
gi 500857552 415 fILAMRGI--GGFFAGIWGGIVDTVKGWF 441
Cdd:PRK10001 368 -LIVMENVeeGGFFSRMWDFVMMKFHQWF 395
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
308-392 |
1.27e-17 |
|
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: 77.64 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 308 FTMKEMYKKGQQIKgheNIEVDKGKDKEVPVVTKEAFSVPVKNGDEKSFKAKVNIEKTKLEAPIKKGTKVGMLTtsYSGD 387
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLV--VTLD 75
|
....*
gi 500857552 388 EKDYG 392
Cdd:smart00936 76 GKLIG 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
10-415 |
1.21e-109 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 326.41 E-value: 1.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 10 MVSILALALIVTAFTPmskAKAAEDPFNVNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWD 89
Cdd:COG1686 1 MKKLLLLALLLLLAAA---AAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 90 QTYTPDDYVYEISqdrsLSNVPLRKDGSYTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKELGLTNYKFV 169
Cdd:COG1686 78 DKVTVSEEAARTG----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 170 NATGLenkdlhgkqpkgtgTDEESEVSAKDMALLAQHLIKDHPEILETSSIAKTKFREGtdDEMDMPNWNfmlkGLVKEY 249
Cdd:COG1686 154 NPTGL--------------PDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTN----RLLGRY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 250 EGVDGLKTGSTDSAGSSFTGTAKQGDMRVIAVILNAKGnlHTARFDVAKKLFDYAFknftmkemyKKGQQIkghenievd 329
Cdd:COG1686 214 PGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGF---------PKGEAL--------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 330 kgkdkevpvvtkeafsvpvkngdeksfKAKVNIEKtKLEAPIKKGTKVGMLTTSYSGdekdygylnKDQSGVELITKTGD 409
Cdd:COG1686 274 ---------------------------KAEVVLDG-PLKAPVKKGQVVGTLVVTLDG---------KTIAEVPLVAAEDV 316
|
....*.
gi 500857552 410 EKANWF 415
Cdd:COG1686 317 EKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
38-286 |
2.67e-82 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 253.08 E-value: 2.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 38 VNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWDQTYTPDDYVYEISQDRSlSNVPLRKDGS 117
Cdd:pfam00768 6 IAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLKPGSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 118 YTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKELGLTNYKFVNATGLENKDLHGkqpkgtgtdeesevSA 197
Cdd:pfam00768 85 VSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYS--------------SA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 198 KDMALLAQHLIKDHPEILETSSIAKTKFREgtddemdMPNWNFMLKGLVKEYEG--VDGLKTGSTDSAGSSFTGTAKQGD 275
Cdd:pfam00768 151 RDMAILAKALIKDLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASATKGG 223
|
250
....*....|.
gi 500857552 276 MRVIAVILNAK 286
Cdd:pfam00768 224 MRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
10-322 |
3.56e-70 |
|
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: 226.40 E-value: 3.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 10 MVSILALALIVTAF------TPMSKAKAAEDPF---NVNAKAAILIeASTGKILYSKNAEQRLPIASMAKMMTEYLLLEA 80
Cdd:NF038258 1 IVSLLLLSTIITPPasaaaeTPVEIANQEGYQNlseQYNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 81 IAEGKVKWDQTYTPDDYVYEISQDRSLSNVPLRKDGSYTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKE 160
Cdd:NF038258 80 IKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 161 LGLTNYKFVNATGLENKDLHGKQPKGTGTDEESEVSAKDMALLAQHLIKDHPEILETssiakTKFREGTDDEMDMPNWNF 240
Cdd:NF038258 160 LGMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKY-----TKLTADTQHGVTLYTTNL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 241 MLKGLVKEYEGVDGLKTGSTDSaGSSFTGTAKQGDMRVIAVILNAK--GNLHT--ARFDVAKKLFDYAFKNFTMKEMYKK 316
Cdd:NF038258 235 SLPGQPMSLKGTDGLKTGTSDE-GYNLALTTKRDGLRINQVIMNVGpyPSEGAkhARNKIANALMERAFKQYEYKKVLSK 313
|
....*..
gi 500857552 317 G-QQIKG 322
Cdd:NF038258 314 GeHKIDG 320
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
17-441 |
1.58e-50 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 175.95 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 17 ALIVTAFTPMSKAKAAEDPFNVNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWDQTYT--P 94
Cdd:PRK10001 16 AFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTvgK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 95 DDYVYEISQDRSLSNVPLRKDGSYTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKELGLTNYKFvnatgl 174
Cdd:PRK10001 96 DAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 175 enKDLHGKQPKGTGTdeesevSAKDMALLAQHLIKDHPEiletsSIAKTKFREGTDDEMDMPNWNFMlkgLVKEYEGVDG 254
Cdd:PRK10001 170 --QTVHGLDAPGQFS------TARDMALLGKALIHDVPE-----EYAIHKEKEFTFNKIRQPNRNRL---LWSSNLNVDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 255 LKTGSTDSAGSSFTGTAKQGDMRVIAVILNAKGNlhTARFDVAKKLFDYAFKNFTMKEMYKKGQQIKgheNIEVDKGKDK 334
Cdd:PRK10001 234 MKTGTTAGAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGFRFFETVTPIKPDATFV---TQRVWFGDKS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 335 EVPVVTKEAFSVPVKNGDEKSFKAKVNIEKTKLEAPIKKGTKVGMLTTSYSGdekdygylnkdqsgvelitKTGDEKAnw 414
Cdd:PRK10001 309 EVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNG-------------------KSIEQRP-- 367
|
410 420
....*....|....*....|....*....
gi 500857552 415 fILAMRGI--GGFFAGIWGGIVDTVKGWF 441
Cdd:PRK10001 368 -LIVMENVeeGGFFSRMWDFVMMKFHQWF 395
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
7-378 |
1.00e-41 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 152.28 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 7 KQLMVSILALALIVTAFTPMSKAKAAEDPFNVNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKV 86
Cdd:PRK11397 3 RRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 87 kwdqtyTPDDYVyEISQDRSLSNVPLRKDGSY---------TVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAK 157
Cdd:PRK11397 83 ------TPDDIV-TVGRDAWAKDNPVFVGSSLmflkegdrvSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 158 AKELGLTNYKFVNATGLENKDLHGkqpkgtgtdeesevSAKDMALLAQHLIKDHPEILETSSIAKTKFREGTDDEMDMPN 237
Cdd:PRK11397 156 VEKLHLKDTHFETVHGLDAPGQHS--------------SAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 238 WNFMLKglvkeyegVDGLKTGSTDSAGSSFTGTAKQGDMRVIAVILNAKGNlhTARFDVAKKLFDYAFKNFTMKEMYKKG 317
Cdd:PRK11397 222 WDKTMN--------VDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSA--KGREEQARKLLRWGQQNFTTVQILHRG 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500857552 318 QQIkGHENIEVdkGKDKEVPVVTKEAFSVPVKNGDEKSFKAKVNIEKTKLEAPIKKGTKVG 378
Cdd:PRK11397 292 KKV-GTERIWY--GDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVG 349
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-386 |
2.85e-36 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 137.68 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 1 MNSKILKQLMVSILALALIVTAFTPMSKAkaaeDPFN----------VNAKAAILIEASTGKILYSKNAEQRLPIASMAK 70
Cdd:PRK10793 1 MKTIFSARIMKRLALTTALCTAFISAAHA----DDLNiktmipgvpqIDAESYILIDYNSGKVLAEQNADVRRDPASLTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 71 MMTEYLLLEAIAEGKVKwdqtytPDDYVyEISQDRSLSNVPLRKDGSY---------TVKELYQATAIYSANAAAIGLAE 141
Cdd:PRK10793 77 MMTSYVIGQAMKAGKFK------ETDLV-TVGNDAWATGNPVFKGSSLmflkpgmqvPVSQLIRGINLQSGNDACVAMAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 142 VIAGSESKFVEKMNAKAKELGLTNYKFvnatglenKDLHGKQPKGTGTdeesevSAKDMALLAQHLIKDHPEiletsSIA 221
Cdd:PRK10793 150 YVAGSQDAFVGLMNSYVNALGLKNTHF--------QTVHGLDADGQYS------SARDMALIGQALIRDVPN-----EYA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 222 KTKFREGTDDEMDMPNWNFML--KGLvkeyeGVDGLKTGSTDSAGSSFTGTAKQGDMRVIAVILNakGNLHTARFDVAKK 299
Cdd:PRK10793 211 IYKEKEFTFNGIRQLNRNGLLwdNSL-----NVDGIKTGHTDKAGYNLVASATEGQMRLISAVMG--GRTFKGRETESKK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 300 LFDYAFKNFTMKEMYKKGQQIKGH-----ENIEVDKGKDKEVpvvtkeAFSVPvkNGDEKSFKAKVNIEKTKLEAPIKKG 374
Cdd:PRK10793 284 LLTWGFRFFETVNPLKVGKEFASEpvwfgDSDRASLGVDKDV------YLTIP--RGRMKDLKASYVLNTSELHAPLQKN 355
|
410
....*....|..
gi 500857552 375 TKVGMLTTSYSG 386
Cdd:PRK10793 356 QVVGTINFQLDG 367
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
11-287 |
4.23e-22 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 95.90 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 11 VSILALALIVTAFTPMSKAKAAE-------DPFNVNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAiae 83
Cdd:PRK11669 5 VSLLSLLLLLAGVPFAPQAVAKTaaattasQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 84 gKVKWDQTYTPDdyvyeISQDRSLSNVPLR-KDGS-YTVKELYQATAIYSANAAAIGLAEVIAGSESKFVEKMNAKAKEL 161
Cdd:PRK11669 82 -KLPLDEKLKVD-----ISQTPEMKGVYSRvRLNSeISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 162 GLTNYKFVNATGLENKDLHgkqpkgtgtdeesevSAKDMALLaqhLI--KDHPEILETSSIAK--TKFRE--------GT 229
Cdd:PRK11669 156 GMTNTRYVEPTGLSIHNVS---------------TARDLTKL---LIasKQYPLIGQLSTTREktATFRKpnytlpfrNT 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 500857552 230 DDEMDMPNWNFMLKglvkeyegvdglKTGSTDSAGSSFTGTAKQGDMRVIAVILNAKG 287
Cdd:PRK11669 218 NHLVYRDNWNIQLT------------KTGFTNAAGHCLVMRTVINNRPVALVVLDAFG 263
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
308-392 |
1.27e-17 |
|
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: 77.64 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 308 FTMKEMYKKGQQIKgheNIEVDKGKDKEVPVVTKEAFSVPVKNGDEKSFKAKVNIEKTKLEAPIKKGTKVGMLTtsYSGD 387
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLV--VTLD 75
|
....*
gi 500857552 388 EKDYG 392
Cdd:smart00936 76 GKLIG 80
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
308-387 |
4.63e-16 |
|
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: 73.01 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 308 FTMKEMYKKGQQIKgheNIEVDKGKDKEVPVVTKEAFSVPVKNGDEKSFKAKVNIEKtKLEAPIKKGTKVGMLTTSYSGD 387
Cdd:pfam07943 1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKK-PLEAPIKKGQVVGKLEVYLDGK 76
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
15-207 |
3.97e-12 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 66.46 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 15 ALALIVTAFTPMSKAKAAEDPFN-----VNAKAAILIEASTGKILYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWD 89
Cdd:COG2367 3 LLALLLLAAAAAAPASALEAELAaleaaLGGRVGVYVLDLDTGETVGINADERFPAASTFKLPVLAAVLRQVDAGKLSLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 90 Q--TYTPDDYVYE--ISQDrslsnvpLRKDGSYTVKELYQATAIYSANAAA------IGLAEViagseskfvekmNAKAK 159
Cdd:COG2367 83 ErvTLTPEDLVGGsgILQK-------LPDGTGLTLRELAELMITVSDNTATnlllrlLGPDAV------------NAFLR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500857552 160 ELGLTNYKFVNATGlenkDLHGKQPKGTGTdeeseVSAKDMALLAQHL 207
Cdd:COG2367 144 SLGLTDTRLDRKEP----DLNELPGDGRNT-----TTPRDMARLLAAL 182
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
49-210 |
7.86e-11 |
|
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: 61.52 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 49 STGKiLYSKNAEQRLPIASMAKMMTEYLLLEAIAEGKVKWDQ--TYTPDDYVyeisqDRSLSNVPLRKDGSYTVKELYQA 126
Cdd:pfam13354 8 DTGE-ELGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDErlTVTAEDKV-----GGSGILQYLPDGSQLSLRDLLTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857552 127 TAIYSANAAA------IGLAEViagseskfvekmNAKAKELGLTNykfvnaTGLENK--DLHGKQPKGTGTdeeseVSAK 198
Cdd:pfam13354 82 MIAVSDNTATnllidrLGLEAV------------NARLRALGLRD------TRLRRKlpDLRAADKGGTNT-----TTAR 138
|
170
....*....|..
gi 500857552 199 DMALLAQHLIKD 210
Cdd:pfam13354 139 DMAKLLEALYRG 150
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
42-91 |
6.13e-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: 6.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500857552 42 AAILIeASTGKILYSK-----NAEQRLP--------IASMAKMMTEYLLLEAIAEGKVKWDQT 91
Cdd:COG1680 35 AAVAV-VRDGKVVYEKaygvaDLETGRPvtpdtlfrIASVTKSFTATAVLQLVEEGKLDLDDP 96
|
|
| |
