|
Name |
Accession |
Description |
Interval |
E-value |
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
1-388 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 854.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 1 MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:PRK11397 1 LKRRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:PRK11397 81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 241 FNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLP 320
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 999850057 321 KAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA 388
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-379 |
1.06e-139 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 400.75 E-value: 1.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 1 MKRRLIIAASLFVFNLSSGfaaenipfSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAA--------PAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 81 RITPDDIVTVGRDAWAkdnpvfVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:COG1686 73 KISLDDKVTVSEEAAR------TGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWN---GITQQNRNGLLWdKTMNVDGLKTGHTS 237
Cdd:COG1686 147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 238 GAGFNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGqqnfttvqilhrgkkvgteriwygdkenidlgteqefwm 317
Cdd:COG1686 226 AAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG--------------------------------------- 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 999850057 318 vLPKAEipHIKAKYTLDGkELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSR 379
Cdd:COG1686 267 -FPKGE--ALKAEVVLDG-PLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
29-262 |
1.55e-131 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 376.34 E-value: 1.55e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 29 PQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPvfvGSSLM 108
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 109 FLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLS 188
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 999850057 189 RAIIHGEPEFYHMYSEKSLTW---NGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGAD 262
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
46-261 |
2.11e-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: 119.70 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 46 TGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTV-GRDAWAKDNPvfvGSSLMFLKEGDRVSVRDLSRG 124
Cdd:NF038258 49 TGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKItSDYEKMSTLP---NLSTFPLKPGQTYTIKELLKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 125 LIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLD-------APGQ-------HSSAYDLAVLSRA 190
Cdd:NF038258 126 TALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADnnllkpyAPKKykdetksKSTAKDMAILSQH 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 999850057 191 IIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTM---NVDGLKTGhTSGAGFNLIASAVDGQRRLIAVVMGA 261
Cdd:NF038258 206 LIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQVIMNV 278
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
282-373 |
3.68e-26 |
|
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: 100.37 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 282 FTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVA 361
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 999850057 362 HWPLVTLESVGE 373
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
1-388 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 854.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 1 MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:PRK11397 1 LKRRLIIAASLFAFNLSSAFAAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:PRK11397 81 RITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 241 FNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLP 320
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 999850057 321 KAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA 388
Cdd:PRK11397 321 KAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
6-386 |
1.60e-155 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 443.91 E-value: 1.60e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 6 IIAASLFVFNLSSGFAAENIPFS---PQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRI 82
Cdd:PRK10793 13 LALTTALCTAFISAAHADDLNIKtmiPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 83 TPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLK 162
Cdd:PRK10793 93 KETDLVTVGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 163 DTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFN 242
Cdd:PRK10793 173 NTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 243 LIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKA 322
Cdd:PRK10793 253 LVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 999850057 323 EIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDY----FHH 386
Cdd:PRK10793 333 RMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYiklmFHH 400
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
3-385 |
2.56e-145 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 417.86 E-value: 2.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 3 RRLIIAASLFVF-NLSSGFAAENIPfspQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHR 81
Cdd:PRK10001 8 LRGLAAGSAFLFlFAPTAFAAEQTV---EAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 82 ITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHL 161
Cdd:PRK10001 85 IKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 162 KDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGF 241
Cdd:PRK10001 165 TNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAGY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 242 NLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPK 321
Cdd:PRK10001 245 NLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPR 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 999850057 322 AEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDY----FH 385
Cdd:PRK10001 325 GQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFvmmkFH 392
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-379 |
1.06e-139 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 400.75 E-value: 1.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 1 MKRRLIIAASLFVFNLSSGfaaenipfSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAA--------PAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 81 RITPDDIVTVGRDAWAkdnpvfVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLH 160
Cdd:COG1686 73 KISLDDKVTVSEEAAR------TGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWN---GITQQNRNGLLWdKTMNVDGLKTGHTS 237
Cdd:COG1686 147 MTNTHFVNPTGLPDPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 238 GAGFNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGqqnfttvqilhrgkkvgteriwygdkenidlgteqefwm 317
Cdd:COG1686 226 AAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYG--------------------------------------- 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 999850057 318 vLPKAEipHIKAKYTLDGkELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSR 379
Cdd:COG1686 267 -FPKGE--ALKAEVVLDG-PLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
29-262 |
1.55e-131 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 376.34 E-value: 1.55e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 29 PQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPvfvGSSLM 108
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 109 FLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLS 188
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 999850057 189 RAIIHGEPEFYHMYSEKSLTW---NGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGAD 262
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
46-261 |
2.11e-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: 119.70 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 46 TGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTV-GRDAWAKDNPvfvGSSLMFLKEGDRVSVRDLSRG 124
Cdd:NF038258 49 TGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKItSDYEKMSTLP---NLSTFPLKPGQTYTIKELLKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 125 LIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLD-------APGQ-------HSSAYDLAVLSRA 190
Cdd:NF038258 126 TALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGADnnllkpyAPKKykdetksKSTAKDMAILSQH 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 999850057 191 IIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTM---NVDGLKTGhTSGAGFNLIASAVDGQRRLIAVVMGA 261
Cdd:NF038258 206 LIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQVIMNV 278
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
282-373 |
3.68e-26 |
|
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: 100.37 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 282 FTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVA 361
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 999850057 362 HWPLVTLESVGE 373
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
282-373 |
9.43e-23 |
|
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: 91.12 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 282 FTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDgKELTAPISAHQRVGEIELYDRDKQVA 361
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLK-KPLEAPIKKGQVVGKLEVYLDGKLIG 79
|
90
....*....|..
gi 999850057 362 HWPLVTLESVGE 373
Cdd:pfam07943 80 EVPLVAKEDVEE 91
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
1-261 |
8.74e-18 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 83.19 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 1 MKRRLIIAASLFVFN----LSSGFAAEN-IPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVdr 75
Cdd:PRK11669 1 MKFRVSLLSLLLLLAgvpfAPQAVAKTAaATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 76 aIDSHrITPDDIVTVGrdawAKDNPVFVGsslMF--LKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMN 153
Cdd:PRK11669 79 -LDAK-LPLDEKLKVD----ISQTPEMKG---VYsrVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 154 NYAEKLHLKDTHFETVHGLdAPGQHSSAYDLAVLSRAiihgePEFYHMYSEKSLT----------WNGITQQNRNGLLWD 223
Cdd:PRK11669 150 AKAKALGMTNTRYVEPTGL-SIHNVSTARDLTKLLIA-----SKQYPLIGQLSTTrektatfrkpNYTLPFRNTNHLVYR 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 999850057 224 KTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGA 261
Cdd:PRK11669 224 DNWNIQLTKTGFTNAAGHCLVMRTVINNRPVALVVLDA 261
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
38-195 |
2.88e-07 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 51.44 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 38 SWVLMDYTTGQILTAgNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPVfvgssLMFLKEGDRVS 117
Cdd:COG2367 36 GVYVLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGI-----LQKLPDGTGLT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 118 VRDLSRGLIVDSGNDACVALADYIaGGQRqfvemMNNYAEKLHLKDTHFE-TVHGL-DAPGQH---SSAYDLAVLSRAII 192
Cdd:COG2367 110 LRELAELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTRLDrKEPDLnELPGDGrntTTPRDMARLLAALY 183
|
...
gi 999850057 193 HGE 195
Cdd:COG2367 184 RGE 186
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
38-195 |
2.77e-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: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 38 SWVLMDYTTGQILtAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDawakdnpVFVGSSLMF--LKEGDR 115
Cdd:pfam13354 1 GIYVRDLDTGEEL-GINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAE-------DKVGGSGILqyLPDGSQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999850057 116 VSVRDLSRGLIVDSGNDACVALADYIAggqrqfVEMMNNYAEKLHLKDTHFE----TVHGLDAPGQH-SSAYDLAVLSRA 190
Cdd:pfam13354 73 LSLRDLLTLMIAVSDNTATNLLIDRLG------LEAVNARLRALGLRDTRLRrklpDLRAADKGGTNtTTARDMAKLLEA 146
|
....*
gi 999850057 191 IIHGE 195
Cdd:pfam13354 147 LYRGE 151
|
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