|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
28-383 |
9.65e-165 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 467.41 E-value: 9.65e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 28 IIPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAKNFPE---SS 104
Cdd:PRK10793 37 MIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVfkgSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 105 KMFIEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDAHYTTPRDMAT 184
Cdd:PRK10793 117 LMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 185 LGAALIRDVPDEYALYKQKSFTFNGIKQYNRNSLLWDESLDVDGIKTGHTSDAGYSLVTSATKNDMRLIAVVMGTSSERA 264
Cdd:PRK10793 197 IGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 265 RKVESKKLLNYGFRFFETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIPRGQHKNLKANFELDDT-LEAPLAKGT 343
Cdd:PRK10793 277 RETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTSeLHAPLQKNQ 356
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 657907274 344 KVGTLFLQLEGEDIAQYPLVTLEEIQEGSFFSKIYDYLRL 383
Cdd:PRK10793 357 VVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKL 396
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
15-376 |
2.18e-146 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 417.70 E-value: 2.18e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 15 LVCSAAVFSATAQIIPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEK 94
Cdd:COG1686 6 LLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 95 AWAKnfpESSKMFIEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDA 174
Cdd:COG1686 86 AART---GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 175 HYTTPRDMATLGAALIRDVPDEYALYKQKSFTFN---GIKQYNRNSLLWdESLDVDGIKTGHTSDAGYSLVTSATKNDMR 251
Cdd:COG1686 163 HYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTDAAGYCLVASAKRGGRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 252 LIAVVMGTSSERARKVESKKLLNYGFrffetitpykagdsfaeqrvwmgnkenvslgiledtpitiPRGQhkNLKANFEL 331
Cdd:COG1686 242 LIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKGE--ALKAEVVL 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 657907274 332 DDTLEAPLAKGTKVGTLFLQLEGEDIAQYPLVTLEEIQEGSFFSK 376
Cdd:COG1686 280 DGPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
30-258 |
5.69e-106 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 311.63 E-value: 5.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 30 PAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAKNFPESSKMFIE 109
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGSSNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 110 VGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDAHYTTPRDMATLGAAL 189
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657907274 190 IRDVPDEYALYKQKSFTF---NGIKQYNRNSLLWDESLDVDGIKTGHTSDAGYSLVTSATKNDMRLIAVVMG 258
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMG 232
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
34-281 |
1.28e-40 |
|
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: 147.05 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 34 QVNAKGYFLVDfTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEK-AWAKNFPESSKMFIEVGK 112
Cdd:NF038258 37 QYNPEGAIVTT-QTGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDyEKMSTLPNLSTFPLKPGQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 113 QVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDT--------------DAHYTT 178
Cdd:NF038258 116 TYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNnllkpyapkkykdeTKSKST 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 179 PRDMATLGAALIRDVPDEYALYKQKSFTFNGIKQYNRNSLLWDESL---DVDGIKTGhTSDAGYSLVTSATKNDMRLIAV 255
Cdd:NF038258 196 AKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQV 274
|
250 260 270
....*....|....*....|....*....|..
gi 657907274 256 VMGTS---SERARKVESK---KLLNYGFRFFE 281
Cdd:NF038258 275 IMNVGpypSEGAKHARNKianALMERAFKQYE 306
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
280-370 |
1.94e-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: 111.92 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 280 FETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIPRGQHKNLKANFELD-DTLEAPLAKGTKVGTLFLQLEGEDIA 358
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDkPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 657907274 359 QYPLVTLEEIQE 370
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
28-383 |
9.65e-165 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 467.41 E-value: 9.65e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 28 IIPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAKNFPE---SS 104
Cdd:PRK10793 37 MIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVfkgSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 105 KMFIEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDAHYTTPRDMAT 184
Cdd:PRK10793 117 LMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 185 LGAALIRDVPDEYALYKQKSFTFNGIKQYNRNSLLWDESLDVDGIKTGHTSDAGYSLVTSATKNDMRLIAVVMGTSSERA 264
Cdd:PRK10793 197 IGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 265 RKVESKKLLNYGFRFFETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIPRGQHKNLKANFELDDT-LEAPLAKGT 343
Cdd:PRK10793 277 RETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTSeLHAPLQKNQ 356
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 657907274 344 KVGTLFLQLEGEDIAQYPLVTLEEIQEGSFFSKIYDYLRL 383
Cdd:PRK10793 357 VVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKL 396
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
26-385 |
2.04e-161 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 458.69 E-value: 2.04e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 26 AQIIPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAKNFPE--- 102
Cdd:PRK10001 28 AEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPAlrg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 103 SSKMFIEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDAHYTTPRDM 182
Cdd:PRK10001 108 SSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQFSTARDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 183 ATLGAALIRDVPDEYALYKQKSFTFNGIKQYNRNSLLWDESLDVDGIKTGHTSDAGYSLVTSATKNDMRLIAVVMGTSSE 262
Cdd:PRK10001 188 ALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 263 RARKVESKKLLNYGFRFFETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIPRGQHKNLKANFELDD-TLEAPLAK 341
Cdd:PRK10001 268 RIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEpQLTAPLKK 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 657907274 342 GTKVGTLFLQLEGEDIAQYPLVTLEEIQEGSFFSKIYDYLRLQI 385
Cdd:PRK10001 348 GQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKF 391
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
15-376 |
2.18e-146 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 417.70 E-value: 2.18e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 15 LVCSAAVFSATAQIIPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEK 94
Cdd:COG1686 6 LLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 95 AWAKnfpESSKMFIEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDA 174
Cdd:COG1686 86 AART---GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 175 HYTTPRDMATLGAALIRDVPDEYALYKQKSFTFN---GIKQYNRNSLLWdESLDVDGIKTGHTSDAGYSLVTSATKNDMR 251
Cdd:COG1686 163 HYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTDAAGYCLVASAKRGGRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 252 LIAVVMGTSSERARKVESKKLLNYGFrffetitpykagdsfaeqrvwmgnkenvslgiledtpitiPRGQhkNLKANFEL 331
Cdd:COG1686 242 LIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKGE--ALKAEVVL 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 657907274 332 DDTLEAPLAKGTKVGTLFLQLEGEDIAQYPLVTLEEIQEGSFFSK 376
Cdd:COG1686 280 DGPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
4-385 |
1.41e-139 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 402.66 E-value: 1.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 4 IKHKILTGVCGLVCSAAVFSATAQI--IPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAG 81
Cdd:PRK11397 1 LKRRLIIAASLFAFNLSSAFAAENIpfSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 82 NIAPTDMVTVSEKAWAKN---FPESSKMFIEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIG 158
Cdd:PRK11397 81 RITPDDIVTVGRDAWAKDnpvFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 159 MTNTHFVNSHGLDTDAHYTTPRDMATLGAALIRDVPDEYALYKQKSFTFNGIKQYNRNSLLWDESLDVDGIKTGHTSDAG 238
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 239 YSLVTSATKNDMRLIAVVMGTSSERARKVESKKLLNYGFRFFETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIP 318
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657907274 319 RGQHKNLKANFELD-DTLEAPLAKGTKVGTLFLQLEGEDIAQYPLVTLEEIQEGSFFSKIYDYLRLQI 385
Cdd:PRK11397 321 KAEIPHIKAKYVLDgKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
30-258 |
5.69e-106 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 311.63 E-value: 5.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 30 PAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAKNFPESSKMFIE 109
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGSSNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 110 VGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDTDAHYTTPRDMATLGAAL 189
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657907274 190 IRDVPDEYALYKQKSFTF---NGIKQYNRNSLLWDESLDVDGIKTGHTSDAGYSLVTSATKNDMRLIAVVMG 258
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMG 232
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
34-281 |
1.28e-40 |
|
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: 147.05 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 34 QVNAKGYFLVDfTTGKVIAQGEADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEK-AWAKNFPESSKMFIEVGK 112
Cdd:NF038258 37 QYNPEGAIVTT-QTGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKITSDyEKMSTLPNLSTFPLKPGQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 113 QVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMNAHAEKIGMTNTHFVNSHGLDT--------------DAHYTT 178
Cdd:NF038258 116 TYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADNnllkpyapkkykdeTKSKST 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 179 PRDMATLGAALIRDVPDEYALYKQKSFTFNGIKQYNRNSLLWDESL---DVDGIKTGhTSDAGYSLVTSATKNDMRLIAV 255
Cdd:NF038258 196 AKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQV 274
|
250 260 270
....*....|....*....|....*....|..
gi 657907274 256 VMGTS---SERARKVESK---KLLNYGFRFFE 281
Cdd:NF038258 275 IMNVGpypSEGAKHARNKianALMERAFKQYE 306
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
280-370 |
8.18e-32 |
|
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: 115.38 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 280 FETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIPRGQHKNLKANFELDDTLEAPLAKGTKVGTLFLQLEGEDIAQ 359
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKPLEAPIKKGQVVGKLEVYLDGKLIGE 80
|
90
....*....|.
gi 657907274 360 YPLVTLEEIQE 370
Cdd:pfam07943 81 VPLVAKEDVEE 91
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
280-370 |
1.94e-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: 111.92 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 280 FETITPYKAGDSFAEQRVWMGNKENVSLGILEDTPITIPRGQHKNLKANFELD-DTLEAPLAKGTKVGTLFLQLEGEDIA 358
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDkPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 657907274 359 QYPLVTLEEIQE 370
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
1-256 |
7.72e-18 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 83.19 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 1 MKsIKHKILTgvCGLVCSAAVFSATA-------QIIPAPPQVNAKGYFLVDFTTGKVIAQGEADTKLAPASLTKMMTSYV 73
Cdd:PRK11669 1 MK-FRVSLLS--LLLLLAGVPFAPQAvaktaaaTTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 74 IgteINAgNIAPTDMVTVSekawAKNFPESSKMF--IEVGKQVSVDDLNHGIIIQSGNDACVAMAEHIAGSESAFADLMN 151
Cdd:PRK11669 78 V---LDA-KLPLDEKLKVD----ISQTPEMKGVYsrVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 152 AHAEKIGMTNTHFVNSHGLDTDaHYTTPRDMATLGAAlIRDVP--DEYALYKQKSFTFNGIKQ----YNRNSLLWDESLD 225
Cdd:PRK11669 150 AKAKALGMTNTRYVEPTGLSIH-NVSTARDLTKLLIA-SKQYPliGQLSTTREKTATFRKPNYtlpfRNTNHLVYRDNWN 227
|
250 260 270
....*....|....*....|....*....|.
gi 657907274 226 VDGIKTGHTSDAGYSLVTSaTKNDMRLIAVV 256
Cdd:PRK11669 228 IQLTKTGFTNAAGHCLVMR-TVINNRPVALV 257
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
39-192 |
1.62e-10 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 61.07 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 39 GYFLVDFTTGKVIAQGeADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAKNFPESSKMfiEVGKQVSVDD 118
Cdd:COG2367 36 GVYVLDLDTGETVGIN-ADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGILQKL--PDGTGLTLRE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657907274 119 LNHGIIIQSGNDACVAMAEHIAGSEsafadlMNAHAEKIGMTNTHFVNS----HGLDTDA-HYTTPRDMATLGAALIRD 192
Cdd:COG2367 113 LAELMITVSDNTATNLLLRLLGPDA------VNAFLRSLGLTDTRLDRKepdlNELPGDGrNTTTPRDMARLLAALYRG 185
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
39-192 |
7.66e-09 |
|
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: 55.36 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 39 GYFLVDFTTGKVIAQGeADTKLAPASLTKMMTSYVIGTEINAGNIAPTDMVTVSEKAWAknfPESSKM-FIEVGKQVSVD 117
Cdd:pfam13354 1 GIYVRDLDTGEELGIN-GDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKV---GGSGILqYLPDGSQLSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657907274 118 DLNHGIIIQSGNDACVAMAEHIAGSEsafadlMNAHAEKIGMTNTHFVN-----SHGLDTDAHYTTPRDMATLGAALIRD 192
Cdd:pfam13354 77 DLLTLMIAVSDNTATNLLIDRLGLEA------VNARLRALGLRDTRLRRklpdlRAADKGGTNTTTARDMAKLLEALYRG 150
|
|
|