|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-404 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 839.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 1 MKTTFSVRFMQRLAVTTALSVAAlSTAAHADDLNIKTMIPGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMT 80
Cdd:PRK10793 1 MKTIFSARIMKRLALTTALCTAF-ISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 81 SYVIGQAMKAGKFKESDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFV 160
Cdd:PRK10793 80 SYVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 161 GLMNSYVTALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQTNRNGLLWDNSLNVD 240
Cdd:PRK10793 160 GLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 241 GIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKAGKEFASEPAWFGDNDRASL 320
Cdd:PRK10793 240 GIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 321 GVDKDIYLTIPRGRMKDLKASYVLNTSELHAPLAKNQVVGTINFQLDGKTIEQRPLVVLEEIQEGNFFGRIIDYIKLMFH 400
Cdd:PRK10793 320 GVDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFH 399
|
....
gi 1755444120 401 HWFG 404
Cdd:PRK10793 400 HWFG 403
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
10-390 |
3.50e-137 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 394.97 E-value: 3.50e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 10 MQRLAVTTALSVAALSTAAHADDlniktmipgvPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMTSYVIGQAMK 89
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAAPAAP----------PDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 90 AGKFKESDLVTIGNDAWATGnpvfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTA 169
Cdd:COG1686 71 AGKISLDDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 170 LGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFN---GIRQTNRNGLLWDNSlNVDGIKTGH 246
Cdd:COG1686 145 LGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 247 TDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFrffetvnplkagkefasepawfgdndraslgvdkdi 326
Cdd:COG1686 224 TDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF------------------------------------ 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755444120 327 yltiPRGRmkDLKASYVLNtSELHAPLAKNQVVGTINFQLDGKTIEQRPLVVLEEIQEGNFFGR 390
Cdd:COG1686 268 ----PKGE--ALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
40-273 |
1.22e-128 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 369.79 E-value: 1.22e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 40 PGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTIGNDAWATGNPvfkGSSLM 119
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 120 FLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTALGLKNTHFQTVHGLDADGQYSSARDMALIG 199
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755444120 200 QALIRDVPNEYSIYKEKEFTF---NGIRQTNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 273
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
44-281 |
2.59e-31 |
|
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: 122.39 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 44 QIDAEAYILIDYNsGKVLAEQNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTIGNDAwatgnpvFKGSSL----- 118
Cdd:NF038258 37 QYNPEGAIVTTQT-GQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDY-------EKMSTLpnlst 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 119 MFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTALGLKNTHFQTVHGLDAD--GQY------- 189
Cdd:NF038258 109 FPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNllKPYapkkykd 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 190 -----SSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQTNRNGLLWDNSL---NVDGIKTGHTDKaGYNLVASATEG 261
Cdd:NF038258 189 etkskSTAKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTGTSDE-GYNLALTTKRD 267
|
250 260
....*....|....*....|
gi 1755444120 262 QMRLISAVMGGRTFKGREAE 281
Cdd:NF038258 268 GLRINQVIMNVGPYPSEGAK 287
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
293-384 |
1.15e-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: 198004 [Multi-domain] Cd Length: 92 Bit Score: 112.69 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 293 FETVNPLKAGKEFASEPAWFGDNDRASLGVDKDIYLTIPRGRMKDLKASYVLNTSELHAPLAKNQVVGTINFQLDGKTIE 372
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 1755444120 373 QRPLVVLEEIQE 384
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-404 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 839.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 1 MKTTFSVRFMQRLAVTTALSVAAlSTAAHADDLNIKTMIPGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMT 80
Cdd:PRK10793 1 MKTIFSARIMKRLALTTALCTAF-ISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 81 SYVIGQAMKAGKFKESDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFV 160
Cdd:PRK10793 80 SYVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 161 GLMNSYVTALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQTNRNGLLWDNSLNVD 240
Cdd:PRK10793 160 GLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 241 GIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKAGKEFASEPAWFGDNDRASL 320
Cdd:PRK10793 240 GIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 321 GVDKDIYLTIPRGRMKDLKASYVLNTSELHAPLAKNQVVGTINFQLDGKTIEQRPLVVLEEIQEGNFFGRIIDYIKLMFH 400
Cdd:PRK10793 320 GVDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFH 399
|
....
gi 1755444120 401 HWFG 404
Cdd:PRK10793 400 HWFG 403
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
10-404 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 563.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 10 MQRLAVTTALSVAALSTAAHADDlniktmIPGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMTSYVIGQAMK 89
Cdd:PRK10001 8 LRGLAAGSAFLFLFAPTAFAAEQ------TVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 90 AGKFKESDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTA 169
Cdd:PRK10001 82 ADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 170 LGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQTNRNGLLWDNSLNVDGIKTGHTDK 249
Cdd:PRK10001 162 LGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 250 AGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKAGKEFASEPAWFGDNDRASLGVDKDIYLT 329
Cdd:PRK10001 242 AGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVT 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755444120 330 IPRGRMKDLKASYVLNTSELHAPLAKNQVVGTINFQLDGKTIEQRPLVVLEEIQEGNFFGRIIDYIKLMFHHWFG 404
Cdd:PRK10001 322 IPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFG 396
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
12-399 |
1.51e-176 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 497.42 E-value: 1.51e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 12 RLAVTTALSVAALSTAAHADDLNIKtmiPGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMTSYVIGQAMKAG 91
Cdd:PRK11397 4 RLIIAASLFAFNLSSAFAAENIPFS---PQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 92 KFKESDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTALG 171
Cdd:PRK11397 81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 172 LKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQTNRNGLLWDNSLNVDGIKTGHTDKAG 251
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 252 YNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKAGKEFASEPAWFGDNDRASLGVDKDIYLTIP 331
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755444120 332 RGRMKDLKASYVLNTSELHAPLAKNQVVGTINFQLDGKTIEQRPLVVLEEIQEGNFFGRIIDYIKLMF 399
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
10-390 |
3.50e-137 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 394.97 E-value: 3.50e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 10 MQRLAVTTALSVAALSTAAHADDlniktmipgvPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMTSYVIGQAMK 89
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAAPAAP----------PDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 90 AGKFKESDLVTIGNDAWATGnpvfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTA 169
Cdd:COG1686 71 AGKISLDDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 170 LGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFN---GIRQTNRNGLLWDNSlNVDGIKTGH 246
Cdd:COG1686 145 LGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 247 TDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFrffetvnplkagkefasepawfgdndraslgvdkdi 326
Cdd:COG1686 224 TDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF------------------------------------ 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755444120 327 yltiPRGRmkDLKASYVLNtSELHAPLAKNQVVGTINFQLDGKTIEQRPLVVLEEIQEGNFFGR 390
Cdd:COG1686 268 ----PKGE--ALKAEVVLD-GPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
40-273 |
1.22e-128 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 369.79 E-value: 1.22e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 40 PGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTIGNDAWATGNPvfkGSSLM 119
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 120 FLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTALGLKNTHFQTVHGLDADGQYSSARDMALIG 199
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755444120 200 QALIRDVPNEYSIYKEKEFTF---NGIRQTNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 273
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
44-281 |
2.59e-31 |
|
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: 122.39 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 44 QIDAEAYILIDYNsGKVLAEQNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTIGNDAwatgnpvFKGSSL----- 118
Cdd:NF038258 37 QYNPEGAIVTTQT-GQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDY-------EKMSTLpnlst 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 119 MFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVTALGLKNTHFQTVHGLDAD--GQY------- 189
Cdd:NF038258 109 FPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNllKPYapkkykd 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 190 -----SSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQTNRNGLLWDNSL---NVDGIKTGHTDKaGYNLVASATEG 261
Cdd:NF038258 189 etkskSTAKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTGTSDE-GYNLALTTKRD 267
|
250 260
....*....|....*....|
gi 1755444120 262 QMRLISAVMGGRTFKGREAE 281
Cdd:NF038258 268 GLRINQVIMNVGPYPSEGAK 287
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
293-384 |
1.15e-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: 198004 [Multi-domain] Cd Length: 92 Bit Score: 112.69 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 293 FETVNPLKAGKEFASEPAWFGDNDRASLGVDKDIYLTIPRGRMKDLKASYVLNTSELHAPLAKNQVVGTINFQLDGKTIE 372
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 1755444120 373 QRPLVVLEEIQE 384
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
293-384 |
1.85e-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: 109.61 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 293 FETVNPLKAGKEFASEPAWFGDNDRASLGVDKDIYLTIPRGRMKDLKASYVLNtSELHAPLAKNQVVGTINFQLDGKTIE 372
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLK-KPLEAPIKKGQVVGKLEVYLDGKLIG 79
|
90
....*....|..
gi 1755444120 373 QRPLVVLEEIQE 384
Cdd:pfam07943 80 EVPLVAKEDVEE 91
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
1-273 |
3.74e-18 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 84.35 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 1 MKTTFSVrfmqrLAVTTALSVAALSTAAHADDlNIKTMIPGVPQIDAEAYILIDYNSGKVLAEQNADARRDPASLTKMMT 80
Cdd:PRK11669 1 MKFRVSL-----LSLLLLLAGVPFAPQAVAKT-AAATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 81 SYVIGQAMKAgkFKESDLVTIGNdawatgNPVFKGsslMF--LKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDA 158
Cdd:PRK11669 75 AMVVLDAKLP--LDEKLKVDISQ------TPEMKG---VYsrVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 159 FVGLMNSYVTALGLKNTHFQTVHGLDADgQYSSARDMALIGQAlIRDVP--NEYSIYKEKEFTFN------GIRQTNRng 230
Cdd:PRK11669 144 FIKAMNAKAKALGMTNTRYVEPTGLSIH-NVSTARDLTKLLIA-SKQYPliGQLSTTREKTATFRkpnytlPFRNTNH-- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1755444120 231 LLWDNSLNVDGIKTGHTDKAGYNLVasategqMRlisAVMGGR 273
Cdd:PRK11669 220 LVYRDNWNIQLTKTGFTNAAGHCLV-------MR---TVINNR 252
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
52-205 |
1.32e-06 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 49.51 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 52 LIDYNSGKVLAeQNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTIGNDAWATGNPVfkgssLMFLKPGMQVPVSQ 131
Cdd:COG2367 39 VLDLDTGETVG-INADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGI-----LQKLPDGTGLTLRE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755444120 132 LIRGINLQSGNDACVAMADYVAGsqDAFvglmNSYVTALGLKNTHFQ----TVHGLDADGQ-YSSARDMALIGQALIRD 205
Cdd:COG2367 113 LAELMITVSDNTATNLLLRLLGP--DAV----NAFLRSLGLTDTRLDrkepDLNELPGDGRnTTTPRDMARLLAALYRG 185
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
62-205 |
3.17e-06 |
|
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: 47.65 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755444120 62 AEQNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTIGNDAWATGNPVFKgsslmFLKPGMQVPVSQLIRGINLQSG 141
Cdd:pfam13354 13 LGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQ-----YLPDGSQLSLRDLLTLMIAVSD 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755444120 142 NDACVAMADYVagSQDAFvglmNSYVTALGLKNTHFQ----TVHGLDADGQ-YSSARDMALIGQALIRD 205
Cdd:pfam13354 88 NTATNLLIDRL--GLEAV----NARLRALGLRDTRLRrklpDLRAADKGGTnTTTARDMAKLLEALYRG 150
|
|
| |
