|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-399 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 818.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 1 MKTSFTARLL----VTALSVAALSTAARADDLNMKTMIPGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTS 76
Cdd:PRK10793 1 MKTIFSARIMkrlaLTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 77 YVIGQAMKAGKFKESDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVS 156
Cdd:PRK10793 81 YVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 157 LMNNYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYREKEFTFNGIRQLNRNGLLWDNSLNVDG 236
Cdd:PRK10793 161 LMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 237 IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTYKGRESESKKLLTWGFRFFETVNPIKAGKEFASEPAWFGDSDRASLG 316
Cdd:PRK10793 241 IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 317 VDKDVYLTIPRGRMKDLKASYVLNNTELHAPLQKNQVVGTINFQLDGKTIDQRPLVVLQEIPEGNFFGKIIDYIKLMFHH 396
Cdd:PRK10793 321 VDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHH 400
|
...
gi 505180633 397 WFG 399
Cdd:PRK10793 401 WFG 403
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-385 |
1.21e-136 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 393.43 E-value: 1.21e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 1 MKTSFTARLLVTALSVAALSTAAraddlnmktmipgaPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVIG 80
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAAPAAP--------------PDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 81 QAMKAGKFKESDLVTVGNDAWATGnpvfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLMNN 160
Cdd:COG1686 67 EALKAGKISLDDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 161 YVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYREKEFTFN---GIRQLNRNGLLWDNSlNVDGI 237
Cdd:COG1686 141 KAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 238 KTGHTDKAGYNLVASATEGQMRLISAVMGGRTYKGRESESKKLLTWGFrffetvnpikagkefasepawfgdsdraslgv 317
Cdd:COG1686 220 KTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF-------------------------------- 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180633 318 dkdvyltiPRGRmkDLKASYVLNNtELHAPLQKNQVVGTINFQLDGKTIDQRPLVVLQEIPEGNFFGK 385
Cdd:COG1686 268 --------PKGE--ALKAEVVLDG-PLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
35-268 |
2.50e-129 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 371.33 E-value: 2.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 35 PGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTVGNDAWATGNPvfkGSSLM 114
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 115 FLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLMNNYVNALGLKNTHFQTVHGLDADGQYSSARDMALIG 194
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180633 195 QALIRDVPNEYSIYREKEFTF---NGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 268
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
288-379 |
8.24e-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: 113.08 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 288 FETVNPIKAGKEFASEPAWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNNTELHAPLQKNQVVGTINFQLDGKTID 367
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 505180633 368 QRPLVVLQEIPE 379
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
53-271 |
3.57e-30 |
|
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: 119.31 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 53 GKVLAENNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTVGNDAwatgnpvFKGSSL-----MFLKPGMQVPVSQL 127
Cdd:NF038258 50 GQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDY-------EKMSTLpnlstFPLKPGQTYTIKEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 128 IRGINLQSGNDACVAMADYVAGSQDAFVSLMNNYVNALGLKNTHFQTVHGLDAD--GQY------------SSARDMALI 193
Cdd:NF038258 123 LKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNllKPYapkkykdetkskSTAKDMAIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 194 GQALIRDVPNEYSIYREKEFTFNGIRQLNRNGLLWDNSL---NVDGIKTGHTDKaGYNLVASATEGQMRLISAVMGGRTY 270
Cdd:NF038258 203 SQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTGTSDE-GYNLALTTKRDGLRINQVIMNVGPY 281
|
.
gi 505180633 271 K 271
Cdd:NF038258 282 P 282
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
1-399 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 818.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 1 MKTSFTARLL----VTALSVAALSTAARADDLNMKTMIPGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTS 76
Cdd:PRK10793 1 MKTIFSARIMkrlaLTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 77 YVIGQAMKAGKFKESDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVS 156
Cdd:PRK10793 81 YVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 157 LMNNYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYREKEFTFNGIRQLNRNGLLWDNSLNVDG 236
Cdd:PRK10793 161 LMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 237 IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTYKGRESESKKLLTWGFRFFETVNPIKAGKEFASEPAWFGDSDRASLG 316
Cdd:PRK10793 241 IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 317 VDKDVYLTIPRGRMKDLKASYVLNNTELHAPLQKNQVVGTINFQLDGKTIDQRPLVVLQEIPEGNFFGKIIDYIKLMFHH 396
Cdd:PRK10793 321 VDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHH 400
|
...
gi 505180633 397 WFG 399
Cdd:PRK10793 401 WFG 403
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
3-399 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 563.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 3 TSFTARLLVTALSVAAL---STAARADDlnmktMIPGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVI 79
Cdd:PRK10001 2 TQYSSLLRGLAAGSAFLflfAPTAFAAE-----QTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 80 GQAMKAGKFKESDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLMN 159
Cdd:PRK10001 77 GQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 160 NYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYREKEFTFNGIRQLNRNGLLWDNSLNVDGIKT 239
Cdd:PRK10001 157 GYAKKLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 240 GHTDKAGYNLVASATEGQMRLISAVMGGRTYKGRESESKKLLTWGFRFFETVNPIKAGKEFASEPAWFGDSDRASLGVDK 319
Cdd:PRK10001 237 GTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 320 DVYLTIPRGRMKDLKASYVLNNTELHAPLQKNQVVGTINFQLDGKTIDQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG 399
Cdd:PRK10001 317 AGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFG 396
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
8-394 |
3.16e-177 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 498.96 E-value: 3.16e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 8 RLLVTA-LSVAALSTAARADDLNMKtmiPGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVIGQAMKAG 86
Cdd:PRK11397 4 RLIIAAsLFAFNLSSAFAAENIPFS---PQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 87 KFKESDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLMNNYVNALG 166
Cdd:PRK11397 81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 167 LKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYREKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAG 246
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 247 YNLVASATEGQMRLISAVMGGRTYKGRESESKKLLTWGFRFFETVNPIKAGKEFASEPAWFGDSDRASLGVDKDVYLTIP 326
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180633 327 RGRMKDLKASYVLNNTELHAPLQKNQVVGTINFQLDGKTIDQRPLVVLQEIPEGNFFGKIIDYIKLMF 394
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-385 |
1.21e-136 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 393.43 E-value: 1.21e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 1 MKTSFTARLLVTALSVAALSTAAraddlnmktmipgaPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVIG 80
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAAPAAP--------------PDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 81 QAMKAGKFKESDLVTVGNDAWATGnpvfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLMNN 160
Cdd:COG1686 67 EALKAGKISLDDKVTVSEEAARTG------GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 161 YVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYREKEFTFN---GIRQLNRNGLLWDNSlNVDGI 237
Cdd:COG1686 141 KAKELGMTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 238 KTGHTDKAGYNLVASATEGQMRLISAVMGGRTYKGRESESKKLLTWGFrffetvnpikagkefasepawfgdsdraslgv 317
Cdd:COG1686 220 KTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF-------------------------------- 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505180633 318 dkdvyltiPRGRmkDLKASYVLNNtELHAPLQKNQVVGTINFQLDGKTIDQRPLVVLQEIPEGNFFGK 385
Cdd:COG1686 268 --------PKGE--ALKAEVVLDG-PLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
35-268 |
2.50e-129 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 371.33 E-value: 2.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 35 PGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTVGNDAWATGNPvfkGSSLM 114
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 115 FLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLMNNYVNALGLKNTHFQTVHGLDADGQYSSARDMALIG 194
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180633 195 QALIRDVPNEYSIYREKEFTF---NGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 268
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
288-379 |
8.24e-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: 113.08 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 288 FETVNPIKAGKEFASEPAWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNNTELHAPLQKNQVVGTINFQLDGKTID 367
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 505180633 368 QRPLVVLQEIPE 379
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
288-379 |
1.61e-30 |
|
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.
Pssm-ID: 429749 [Multi-domain] Cd Length: 91 Bit Score: 112.30 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 288 FETVNPIKAGKEFASEPAWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNNtELHAPLQKNQVVGTINFQLDGKTID 367
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKK-PLEAPIKKGQVVGKLEVYLDGKLIG 79
|
90
....*....|..
gi 505180633 368 QRPLVVLQEIPE 379
Cdd:pfam07943 80 EVPLVAKEDVEE 91
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
53-271 |
3.57e-30 |
|
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: 119.31 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 53 GKVLAENNADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTVGNDAwatgnpvFKGSSL-----MFLKPGMQVPVSQL 127
Cdd:NF038258 50 GQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDY-------EKMSTLpnlstFPLKPGQTYTIKEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 128 IRGINLQSGNDACVAMADYVAGSQDAFVSLMNNYVNALGLKNTHFQTVHGLDAD--GQY------------SSARDMALI 193
Cdd:NF038258 123 LKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNNllKPYapkkykdetkskSTAKDMAIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 194 GQALIRDVPNEYSIYREKEFTFNGIRQLNRNGLLWDNSL---NVDGIKTGHTDKaGYNLVASATEGQMRLISAVMGGRTY 270
Cdd:NF038258 203 SQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTGTSDE-GYNLALTTKRDGLRINQVIMNVGPY 281
|
.
gi 505180633 271 K 271
Cdd:NF038258 282 P 282
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
1-268 |
6.25e-18 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 83.58 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 1 MKTSFTARLLVTALSVAALSTAARADDlNMKTMIPGAPQIDAESWVLIDYNSGKVLAENNADARRDPASLTKMMTSYVIG 80
Cdd:PRK11669 1 MKFRVSLLSLLLLLAGVPFAPQAVAKT-AAATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 81 QAMKAgkFKESDLVTVGNdawatgNPVFKGsslMF--LKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVSLM 158
Cdd:PRK11669 80 DAKLP--LDEKLKVDISQ------TPEMKG---VYsrVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 159 NNYVNALGLKNTHFQTVHGLDADgQYSSARDMALIGQAlIRDVP--NEYSIYREKEFTFN------GIRqlNRNGLLWDN 230
Cdd:PRK11669 149 NAKAKALGMTNTRYVEPTGLSIH-NVSTARDLTKLLIA-SKQYPliGQLSTTREKTATFRkpnytlPFR--NTNHLVYRD 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 505180633 231 SLNVDGIKTGHTDKAGYNLVasategqMRlisAVMGGR 268
Cdd:PRK11669 225 NWNIQLTKTGFTNAAGHCLV-------MR---TVINNR 252
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
44-200 |
2.70e-06 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 48.36 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 44 SWVLIDYNSGKVLAENnADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTVGNDAWATGNPVfkgssLMFLKPGMQVP 123
Cdd:COG2367 36 GVYVLDLDTGETVGIN-ADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGI-----LQKLPDGTGLT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 124 VSQLIRGINLQSGNDACVAMADYVAGsqDAFvslmNNYVNALGLKNTHFQ----TVHGLDADGQ-YSSARDMALIGQALI 198
Cdd:COG2367 110 LRELAELMITVSDNTATNLLLRLLGP--DAV----NAFLRSLGLTDTRLDrkepDLNELPGDGRnTTTPRDMARLLAALY 183
|
..
gi 505180633 199 RD 200
Cdd:COG2367 184 RG 185
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
44-200 |
3.26e-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: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 44 SWVLIDYNSGKVLAENnADARRDPASLTKMMTSYVIGQAMKAGKFKESDLVTVGNDAWATGNPVFKgsslmFLKPGMQVP 123
Cdd:pfam13354 1 GIYVRDLDTGEELGIN-GDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQ-----YLPDGSQLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180633 124 VSQLIRGINLQSGNDACVAMADYVagSQDAFvslmNNYVNALGLKNTHFQ----TVHGLDADGQ-YSSARDMALIGQALI 198
Cdd:pfam13354 75 LRDLLTLMIAVSDNTATNLLIDRL--GLEAV----NARLRALGLRDTRLRrklpDLRAADKGGTnTTTARDMAKLLEALY 148
|
..
gi 505180633 199 RD 200
Cdd:pfam13354 149 RG 150
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