|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
4-367 |
1.02e-156 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 443.51 E-value: 1.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 4 RIIACSFLLLCAGLAQAQsliPAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDK 83
Cdd:COG1686 3 KLLLLALLLLLAAAAAAP---AAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 84 VRISEKAWRKGGSKMFVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGWP 163
Cdd:COG1686 80 VTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 164 AEGHMTTARDLGILARALIANHPEHYDIYSEKYFSYS---GINQPNRNRLLWRDSAVDGIKTGHTEEAGYCLVASAMKRG 240
Cdd:COG1686 160 DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 241 MRLIAIVVGTDSDEKRASETQKLLAYGFryyqthkvygqgevlqtervwggkepnvgiavekdifvtiPRGgeEGIKADL 320
Cdd:COG1686 240 RRLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKG--EALKAEV 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 521081556 321 IVDGELEAPIKKGQPVGKVVVTLDGQTVADVKAVAAEDVERAGFFKR 367
Cdd:COG1686 278 VLDGPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
7-370 |
3.91e-118 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 348.52 E-value: 3.91e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 7 ACSFLLLCAGLAQAQSLIPAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRI 86
Cdd:PRK10001 14 GSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 87 SEKAWR------KGGSKMFVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNAT 160
Cdd:PRK10001 94 GKDAWAtgnpalRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 161 GWPAEGHMTTARDLGILARALIANHPEHYDIYSEKYFSYSGINQPNRNRLLWRDSA-VDGIKTGHTEEAGYCLVASAMKR 239
Cdd:PRK10001 174 GLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLnVDGMKTGTTAGAGYNLVASATQG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 240 GMRLIAIVVGTDSDEKRASETQKLLAYGFRYYQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKAD 319
Cdd:PRK10001 254 DMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKAS 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 521081556 320 LIV-DGELEAPIKKGQPVGKVVVTLDGQTVADVKAVAAEDVERAGFFKRMWD 370
Cdd:PRK10001 334 YTLtEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWD 385
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
25-251 |
2.32e-101 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 299.69 E-value: 2.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 25 PAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRISEKAWRKGG---SKMFVK 101
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 102 VGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGWPAEGHMTTARDLGILARAL 181
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521081556 182 IANHPEHYDIYSEKYFSYS---GINQPNRNRLLWRDS-AVDGIKTGHTEEAGYCLVASAMKRGMRLIAIVVGTD 251
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFRginKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
38-281 |
1.65e-38 |
|
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: 141.27 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 38 VDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRISEKAWR----KGGSKMFVKVGDQVPVMDLMR 113
Cdd:NF038258 45 VTTQTGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDYEKmstlPNLSTFPLKPGQTYTIKELLK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 114 GVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGwpAEGHM----------------TTARDLGIL 177
Cdd:NF038258 125 QTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSG--ADNNLlkpyapkkykdetkskSTAKDMAIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 178 ARALIANHPEHYDIYSEKYFSYSGINQPNRNRLL--WRDS--AVDGIKTGhTEEAGYCLVASAMKRGMRLIAIV--VGTD 251
Cdd:NF038258 203 SQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLpgQPMSlkGTDGLKTG-TSDEGYNLALTTKRDGLRINQVImnVGPY 281
|
250 260 270
....*....|....*....|....*....|....
gi 521081556 252 SDEKRASETQK----LLAYGFRYYQTHKVYGQGE 281
Cdd:NF038258 282 PSEGAKHARNKianaLMERAFKQYEYKKVLSKGE 315
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
271-361 |
9.41e-29 |
|
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: 107.30 E-value: 9.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 271 YQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKADLIVDG-ELEAPIKKGQPVGKVVVTLDGQTVA 349
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKpELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 521081556 350 DVKAVAAEDVER 361
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
4-367 |
1.02e-156 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 443.51 E-value: 1.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 4 RIIACSFLLLCAGLAQAQsliPAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDK 83
Cdd:COG1686 3 KLLLLALLLLLAAAAAAP---AAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 84 VRISEKAWRKGGSKMFVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGWP 163
Cdd:COG1686 80 VTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 164 AEGHMTTARDLGILARALIANHPEHYDIYSEKYFSYS---GINQPNRNRLLWRDSAVDGIKTGHTEEAGYCLVASAMKRG 240
Cdd:COG1686 160 DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYPGVDGLKTGYTDAAGYCLVASAKRGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 241 MRLIAIVVGTDSDEKRASETQKLLAYGFryyqthkvygqgevlqtervwggkepnvgiavekdifvtiPRGgeEGIKADL 320
Cdd:COG1686 240 RRLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKG--EALKAEV 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 521081556 321 IVDGELEAPIKKGQPVGKVVVTLDGQTVADVKAVAAEDVERAGFFKR 367
Cdd:COG1686 278 VLDGPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
7-370 |
3.91e-118 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 348.52 E-value: 3.91e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 7 ACSFLLLCAGLAQAQSLIPAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRI 86
Cdd:PRK10001 14 GSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 87 SEKAWR------KGGSKMFVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNAT 160
Cdd:PRK10001 94 GKDAWAtgnpalRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 161 GWPAEGHMTTARDLGILARALIANHPEHYDIYSEKYFSYSGINQPNRNRLLWRDSA-VDGIKTGHTEEAGYCLVASAMKR 239
Cdd:PRK10001 174 GLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLnVDGMKTGTTAGAGYNLVASATQG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 240 GMRLIAIVVGTDSDEKRASETQKLLAYGFRYYQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKAD 319
Cdd:PRK10001 254 DMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKAS 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 521081556 320 LIV-DGELEAPIKKGQPVGKVVVTLDGQTVADVKAVAAEDVERAGFFKRMWD 370
Cdd:PRK10001 334 YTLtEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWD 385
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
21-373 |
1.17e-117 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 347.23 E-value: 1.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 21 QSLIPAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRISEKAWR------KG 94
Cdd:PRK10793 35 KTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWAtgnpvfKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 95 GSKMFVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGWPAEGHMTTARDL 174
Cdd:PRK10793 115 SSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDM 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 175 GILARALIANHPEHYDIYSEKYFSYSGINQPNRNRLLWRDS-AVDGIKTGHTEEAGYCLVASAMKRGMRLIAIVVGTDSD 253
Cdd:PRK10793 195 ALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSlNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 254 EKRASETQKLLAYGFRYYQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKADLIVDG-ELEAPIKK 332
Cdd:PRK10793 275 KGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTsELHAPLQK 354
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 521081556 333 GQPVGKVVVTLDGQTVADVKAVAAEDVERAGFFKRMWDSIK 373
Cdd:PRK10793 355 NQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIK 395
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
9-374 |
5.51e-109 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 324.85 E-value: 5.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 9 SFLLLCAGLAQAQSLIPAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRISE 88
Cdd:PRK11397 13 AFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 89 KAWRK------GGSKMFVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGW 162
Cdd:PRK11397 93 DAWAKdnpvfvGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 163 PAEGHMTTARDLGILARALIANHPEHYDIYSEKYFSYSGINQPNRNRLLWRDSA-VDGIKTGHTEEAGYCLVASAMKRGM 241
Cdd:PRK11397 173 DAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMnVDGLKTGHTSGAGFNLIASAVDGQR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 242 RLIAIVVGTDSDEKRASETQKLLAYGFRYYQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKADLI 321
Cdd:PRK11397 253 RLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYV 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 521081556 322 VDG-ELEAPIKKGQPVGKVVVTLDGQTVADVKAVAAEDVERAGFFKRMWDSIKR 374
Cdd:PRK11397 333 LDGkELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHH 386
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
25-251 |
2.32e-101 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 299.69 E-value: 2.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 25 PAPPQLAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRISEKAWRKGG---SKMFVK 101
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 102 VGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGWPAEGHMTTARDLGILARAL 181
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521081556 182 IANHPEHYDIYSEKYFSYS---GINQPNRNRLLWRDS-AVDGIKTGHTEEAGYCLVASAMKRGMRLIAIVVGTD 251
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFRginKINQRNRNGLLWDKTwNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
38-281 |
1.65e-38 |
|
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: 141.27 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 38 VDANTGQVLVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRISEKAWR----KGGSKMFVKVGDQVPVMDLMR 113
Cdd:NF038258 45 VTTQTGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDYEKmstlPNLSTFPLKPGQTYTIKELLK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 114 GVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLGMENTNFVNATGwpAEGHM----------------TTARDLGIL 177
Cdd:NF038258 125 QTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSG--ADNNLlkpyapkkykdetkskSTAKDMAIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 178 ARALIANHPEHYDIYSEKYFSYSGINQPNRNRLL--WRDS--AVDGIKTGhTEEAGYCLVASAMKRGMRLIAIV--VGTD 251
Cdd:NF038258 203 SQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLpgQPMSlkGTDGLKTG-TSDEGYNLALTTKRDGLRINQVImnVGPY 281
|
250 260 270
....*....|....*....|....*....|....
gi 521081556 252 SDEKRASETQK----LLAYGFRYYQTHKVYGQGE 281
Cdd:NF038258 282 PSEGAKHARNKianaLMERAFKQYEYKKVLSKGE 315
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
1-248 |
1.89e-31 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 120.94 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 1 MITRIIACSFLLLCAGL--------AQAQSLIPAPPQ-LAATSYLLVDANTGQVLVEHEADKEVPPASLTKMMTAYIVSE 71
Cdd:PRK11669 1 MKFRVSLLSLLLLLAGVpfapqavaKTAAATTASQPQeIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 72 EMLkgSIKEDDKVRISEKAWRKG-GSKmfVKVGDQVPVMDLMRGVIIQSGNDASIALAEHVSGSEEVFAEVMNQQAELLG 150
Cdd:PRK11669 81 AKL--PLDEKLKVDISQTPEMKGvYSR--VRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 151 MENTNFVNATGWpAEGHMTTARDLGILaraLIANhpEHYDIYS------EKYFSYSGINQP----NRNRLLWRDS-AVDG 219
Cdd:PRK11669 157 MTNTRYVEPTGL-SIHNVSTARDLTKL---LIAS--KQYPLIGqlsttrEKTATFRKPNYTlpfrNTNHLVYRDNwNIQL 230
|
250 260 270
....*....|....*....|....*....|.
gi 521081556 220 IKTGHTEEAGYCLVasaMKRGM--RLIAIVV 248
Cdd:PRK11669 231 TKTGFTNAAGHCLV---MRTVInnRPVALVV 258
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
271-361 |
6.45e-29 |
|
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: 107.68 E-value: 6.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 271 YQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKADLIVDGELEAPIKKGQPVGKVVVTLDGQTVAD 350
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKPLEAPIKKGQVVGKLEVYLDGKLIGE 80
|
90
....*....|.
gi 521081556 351 VKAVAAEDVER 361
Cdd:pfam07943 81 VPLVAKEDVEE 91
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
271-361 |
9.41e-29 |
|
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: 107.30 E-value: 9.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 271 YQTHKVYGQGEVLQTERVWGGKEPNVGIAVEKDIFVTIPRGGEEGIKADLIVDG-ELEAPIKKGQPVGKVVVTLDGQTVA 349
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKpELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 521081556 350 DVKAVAAEDVER 361
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
3-181 |
2.23e-10 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 60.68 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 3 TRIIAcsFLLLCAGLAQAQSLIPAppQLAA--------TSYLLVDANTGQVlVEHEADKEVPPASLTKMMTAYIVSEEML 74
Cdd:COG2367 1 MRLLA--LLLLAAAAAAPASALEA--ELAAleaalggrVGVYVLDLDTGET-VGINADERFPAASTFKLPVLAAVLRQVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 75 KGSIKEDDKVRIsEKAWRKGGSKMFVK--VGDQVPVMDLMRGVIIQSGNDASIALAEHVsGSEEVfaevmNQQAELLGME 152
Cdd:COG2367 76 AGKLSLDERVTL-TPEDLVGGSGILQKlpDGTGLTLRELAELMITVSDNTATNLLLRLL-GPDAV-----NAFLRSLGLT 148
|
170 180 190
....*....|....*....|....*....|....
gi 521081556 153 NTNFVN----ATGWPAEG-HMTTARDLGILARAL 181
Cdd:COG2367 149 DTRLDRkepdLNELPGDGrNTTTPRDMARLLAAL 182
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
34-182 |
4.89e-10 |
|
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.
Pssm-ID: 463854 [Multi-domain] Cd Length: 215 Bit Score: 58.83 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521081556 34 SYLLVDANTGQVlVEHEADKEVPPASLTKMMTAYIVSEEMLKGSIKEDDKVRIsEKAWRKGGSKMF--VKVGDQVPVMDL 111
Cdd:pfam13354 1 GIYVRDLDTGEE-LGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTV-TAEDKVGGSGILqyLPDGSQLSLRDL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521081556 112 MRGVIIQSGNDASIALAEHVsGSEEVfaevmNQQAELLGMENTNF------VNATGWPAEGhMTTARDLGILARALI 182
Cdd:pfam13354 79 LTLMIAVSDNTATNLLIDRL-GLEAV-----NARLRALGLRDTRLrrklpdLRAADKGGTN-TTTARDMAKLLEALY 148
|
|
| |
