|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
7-416 |
3.55e-117 |
|
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.
Pssm-ID: 468443 [Multi-domain] Cd Length: 407 Bit Score: 348.40 E-value: 3.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 7 KQLLMSLVvltlavTCLAPMSKAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKV 86
Cdd:NF038273 1 KKLILLLL------LLLAFFLATTVSADDFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 87 KWDQTYTPDDYVYEISQDNSLSNVPLRKDgKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDY 166
Cdd:NF038273 75 SWDTPVKISDYPYELTTNYEISNVPLDAR-KYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 167 KFVNATGLENKDLHGHQPEGTSEDEESEVSAKDMAILADHLITDYPEILETSSIAKTKFrkgtdDEMDMPNWNFMLKGLv 246
Cdd:NF038273 154 KLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADF-----AGTTIYSYNYMLKGM- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 247 sEYKKATVDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGNL--HTGRFDETKKMFDYAFDNFSMKEIYAEGDQVKG 324
Cdd:NF038273 228 -PYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNADedEYARFTATNQLLDYIYQNFEKVTLVKKGQAYKD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 325 hKTISVDKGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLTaeytgdekdygFLNSNLAG-- 402
Cdd:NF038273 307 -SKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKKELTAPIKKGQVVGKAT-----------FKDKDLIGkg 374
|
410 420
....*....|....*....|.
gi 518542772 403 -------ADLVTKENVEKANW 416
Cdd:NF038273 375 ylgeppsVELVAKKDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
15-417 |
9.39e-98 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 295.98 E-value: 9.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 15 VLTLAVTCLAPMSkAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTP 94
Cdd:COG1686 4 LLLLALLLLLAAA-AAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 95 DDYVYEISqdnsLSNVPLRKDGKYTVEELYQ--------------AtaiysanaaaiaiaEVVAGSETKFVEKMNAKAKE 160
Cdd:COG1686 83 SEEAARTG----GSKMGLKPGEQVTVEDLLKglllqsgndaavalA--------------EHIAGSEEAFVALMNAKAKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 161 LGLTDYKFVNATGLENKdlhGHQpegtsedeeseVSAKDMAILADHLITDYPEILETSSIAKTKFRKGtdDEMDMPNWNF 240
Cdd:COG1686 145 LGMTNTHFVNPTGLPDP---GHY-----------STARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 241 MLkglvseYKKATVDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGnlHTGRFDETKKMFDYAFdnfsmkeiyaegd 320
Cdd:COG1686 209 LL------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGF------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 321 qvkghktisvdkgkekevgivtnkafslpvKNGEEknYKAKVTLNKEtLTAPVKKGTKVGKLTAEYTGDEkdygflnsnL 400
Cdd:COG1686 268 ------------------------------PKGEA--LKAEVVLDGP-LKAPVKKGQVVGTLVVTLDGKT---------I 305
|
410
....*....|....*..
gi 518542772 401 AGADLVTKENVEKANWF 417
Cdd:COG1686 306 AEVPLVAAEDVEKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
35-288 |
1.52e-74 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 233.05 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 35 PIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTPDDYVYEISQDNSlSNVPLRK 114
Cdd:pfam00768 3 APEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 115 DGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDYKFVNATGLENKDLHGhqpegtsedeese 194
Cdd:pfam00768 82 GSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYS------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 195 vSAKDMAILADHLITDYPEILETSSIAKTKFRkgtddemDMPNWNFMLKGLVSEYKKATVDGLKTGSTDSAGSCFTGTAE 274
Cdd:pfam00768 149 -SARDMAILAKALIKDLPEELSITKEKSFTFR-------GINKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASAT 220
|
250
....*....|....
gi 518542772 275 LNGMRVITVVLNAK 288
Cdd:pfam00768 221 KGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
13-332 |
6.21e-54 |
|
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: 184.02 E-value: 6.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 13 LVVLTLAVTCLAPmSKAKAASDPIDI-------------NASAAIMIeASSGKILYSKNADKRLPIASMTKMMTEYLLLE 79
Cdd:NF038258 1 IVSLLLLSTIITP-PASAAAETPVEIanqegyqnlseqyNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 80 AIDQGKVKWDQTYTPDDYVYEISQDNSLSNVPLRKDGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAK 159
Cdd:NF038258 79 AIKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 160 ELGLTDYKFVNATGLENKDLHGHQPEGTSEDEESEVSAKDMAILADHLITDYPEILETssiakTKFRKGTDDEMDMPNWN 239
Cdd:NF038258 159 ALGMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKY-----TKLTADTQHGVTLYTTN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 240 FMLKGLVSEYKKatVDGLKTGSTDSAGScFTGTAELNGMRVITVVLNAKGNLHTGRFDETKKM----FDYAFDNFSMKEI 315
Cdd:NF038258 234 LSLPGQPMSLKG--TDGLKTGTSDEGYN-LALTTKRDGLRINQVIMNVGPYPSEGAKHARNKIanalMERAFKQYEYKKV 310
|
330
....*....|....*..
gi 518542772 316 YAEGDQVKGHKTISVDK 332
Cdd:NF038258 311 LSKGEHKIDGKTYYVKK 327
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
23-443 |
6.98e-46 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 163.62 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 23 LAPMSKAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTpddyvyeIS 102
Cdd:PRK10001 22 APTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVT-------VG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 103 QDNSLSNVP---------LRKDGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDYKFvnatg 173
Cdd:PRK10001 95 KDAWATGNPalrgssvmfLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 174 lenKDLHGHQPEGTSEdeesevSAKDMAILADHLITDYPEiletsSIAKTKFRKGTDDEMDMPNWNFMLKGlvseyKKAT 253
Cdd:PRK10001 170 ---QTVHGLDAPGQFS------TARDMALLGKALIHDVPE-----EYAIHKEKEFTFNKIRQPNRNRLLWS-----SNLN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 254 VDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGNlhTGRFDETKKMFDYAFDNF-SMKEIYAEGDQVkghkTISVDK 332
Cdd:PRK10001 231 VDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGFRFFeTVTPIKPDATFV----TQRVWF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 333 GKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLtaeytgdekDYGFLNSNLAGADLVTKENVE 412
Cdd:PRK10001 305 GDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTI---------DFQLNGKSIEQRPLIVMENVE 375
|
410 420 430
....*....|....*....|....*....|.
gi 518542772 413 KanwfvltmrsiGGFFAGIWGSIVDTVTGWF 443
Cdd:PRK10001 376 E-----------GGFFSRMWDFVMMKFHQWF 395
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
310-413 |
8.54e-21 |
|
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: 86.50 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 310 FSMKEIYAEGDQVKghkTISVDKGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLTaeYTGD 389
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLV--VTLD 75
|
90 100
....*....|....*....|....
gi 518542772 390 EKDygflnsnLAGADLVTKENVEK 413
Cdd:smart00936 76 GKL-------IGEVPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
7-416 |
3.55e-117 |
|
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.
Pssm-ID: 468443 [Multi-domain] Cd Length: 407 Bit Score: 348.40 E-value: 3.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 7 KQLLMSLVvltlavTCLAPMSKAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKV 86
Cdd:NF038273 1 KKLILLLL------LLLAFFLATTVSADDFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 87 KWDQTYTPDDYVYEISQDNSLSNVPLRKDgKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDY 166
Cdd:NF038273 75 SWDTPVKISDYPYELTTNYEISNVPLDAR-KYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 167 KFVNATGLENKDLHGHQPEGTSEDEESEVSAKDMAILADHLITDYPEILETSSIAKTKFrkgtdDEMDMPNWNFMLKGLv 246
Cdd:NF038273 154 KLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADF-----AGTTIYSYNYMLKGM- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 247 sEYKKATVDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGNL--HTGRFDETKKMFDYAFDNFSMKEIYAEGDQVKG 324
Cdd:NF038273 228 -PYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNADedEYARFTATNQLLDYIYQNFEKVTLVKKGQAYKD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 325 hKTISVDKGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLTaeytgdekdygFLNSNLAG-- 402
Cdd:NF038273 307 -SKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKKELTAPIKKGQVVGKAT-----------FKDKDLIGkg 374
|
410 420
....*....|....*....|.
gi 518542772 403 -------ADLVTKENVEKANW 416
Cdd:NF038273 375 ylgeppsVELVAKKDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
15-417 |
9.39e-98 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 295.98 E-value: 9.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 15 VLTLAVTCLAPMSkAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTP 94
Cdd:COG1686 4 LLLLALLLLLAAA-AAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 95 DDYVYEISqdnsLSNVPLRKDGKYTVEELYQ--------------AtaiysanaaaiaiaEVVAGSETKFVEKMNAKAKE 160
Cdd:COG1686 83 SEEAARTG----GSKMGLKPGEQVTVEDLLKglllqsgndaavalA--------------EHIAGSEEAFVALMNAKAKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 161 LGLTDYKFVNATGLENKdlhGHQpegtsedeeseVSAKDMAILADHLITDYPEILETSSIAKTKFRKGtdDEMDMPNWNF 240
Cdd:COG1686 145 LGMTNTHFVNPTGLPDP---GHY-----------STARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 241 MLkglvseYKKATVDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGnlHTGRFDETKKMFDYAFdnfsmkeiyaegd 320
Cdd:COG1686 209 LL------GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS--EKARFADAAKLLDYGF------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 321 qvkghktisvdkgkekevgivtnkafslpvKNGEEknYKAKVTLNKEtLTAPVKKGTKVGKLTAEYTGDEkdygflnsnL 400
Cdd:COG1686 268 ------------------------------PKGEA--LKAEVVLDGP-LKAPVKKGQVVGTLVVTLDGKT---------I 305
|
410
....*....|....*..
gi 518542772 401 AGADLVTKENVEKANWF 417
Cdd:COG1686 306 AEVPLVAAEDVEKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
35-288 |
1.52e-74 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 233.05 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 35 PIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTPDDYVYEISQDNSlSNVPLRK 114
Cdd:pfam00768 3 APEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 115 DGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDYKFVNATGLENKDLHGhqpegtsedeese 194
Cdd:pfam00768 82 GSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYS------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 195 vSAKDMAILADHLITDYPEILETSSIAKTKFRkgtddemDMPNWNFMLKGLVSEYKKATVDGLKTGSTDSAGSCFTGTAE 274
Cdd:pfam00768 149 -SARDMAILAKALIKDLPEELSITKEKSFTFR-------GINKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASAT 220
|
250
....*....|....
gi 518542772 275 LNGMRVITVVLNAK 288
Cdd:pfam00768 221 KGGMRLISVVMGAF 234
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
13-332 |
6.21e-54 |
|
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: 184.02 E-value: 6.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 13 LVVLTLAVTCLAPmSKAKAASDPIDI-------------NASAAIMIeASSGKILYSKNADKRLPIASMTKMMTEYLLLE 79
Cdd:NF038258 1 IVSLLLLSTIITP-PASAAAETPVEIanqegyqnlseqyNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 80 AIDQGKVKWDQTYTPDDYVYEISQDNSLSNVPLRKDGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAK 159
Cdd:NF038258 79 AIKKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 160 ELGLTDYKFVNATGLENKDLHGHQPEGTSEDEESEVSAKDMAILADHLITDYPEILETssiakTKFRKGTDDEMDMPNWN 239
Cdd:NF038258 159 ALGMKHTHFTNPSGADNNLLKPYAPKKYKDETKSKSTAKDMAILSQHLIKKHPKILKY-----TKLTADTQHGVTLYTTN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 240 FMLKGLVSEYKKatVDGLKTGSTDSAGScFTGTAELNGMRVITVVLNAKGNLHTGRFDETKKM----FDYAFDNFSMKEI 315
Cdd:NF038258 234 LSLPGQPMSLKG--TDGLKTGTSDEGYN-LALTTKRDGLRINQVIMNVGPYPSEGAKHARNKIanalMERAFKQYEYKKV 310
|
330
....*....|....*..
gi 518542772 316 YAEGDQVKGHKTISVDK 332
Cdd:NF038258 311 LSKGEHKIDGKTYYVKK 327
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
23-443 |
6.98e-46 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 163.62 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 23 LAPMSKAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTpddyvyeIS 102
Cdd:PRK10001 22 APTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVT-------VG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 103 QDNSLSNVP---------LRKDGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDYKFvnatg 173
Cdd:PRK10001 95 KDAWATGNPalrgssvmfLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTF----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 174 lenKDLHGHQPEGTSEdeesevSAKDMAILADHLITDYPEiletsSIAKTKFRKGTDDEMDMPNWNFMLKGlvseyKKAT 253
Cdd:PRK10001 170 ---QTVHGLDAPGQFS------TARDMALLGKALIHDVPE-----EYAIHKEKEFTFNKIRQPNRNRLLWS-----SNLN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 254 VDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGNlhTGRFDETKKMFDYAFDNF-SMKEIYAEGDQVkghkTISVDK 332
Cdd:PRK10001 231 VDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGFRFFeTVTPIKPDATFV----TQRVWF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 333 GKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLtaeytgdekDYGFLNSNLAGADLVTKENVE 412
Cdd:PRK10001 305 GDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTI---------DFQLNGKSIEQRPLIVMENVE 375
|
410 420 430
....*....|....*....|....*....|.
gi 518542772 413 KanwfvltmrsiGGFFAGIWGSIVDTVTGWF 443
Cdd:PRK10001 376 E-----------GGFFSRMWDFVMMKFHQWF 395
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
16-417 |
7.00e-38 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 141.88 E-value: 7.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 16 LTLAVTCLAPMSKAKAASDPID-------INASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVkw 88
Cdd:PRK11397 5 LIIAASLFAFNLSSAFAAENIPfspqppaIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 89 dqtyTPDDYVY----EISQDNSL---SNVPLRKDG-KYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKE 160
Cdd:PRK11397 83 ----TPDDIVTvgrdAWAKDNPVfvgSSLMFLKEGdRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 161 LGLTDYKFVNATGLENKDLHGhqpegtsedeesevSAKDMAILADHLITDYPEILETSSiaktkfrkgtddEMDMpNWNF 240
Cdd:PRK11397 159 LHLKDTHFETVHGLDAPGQHS--------------SAYDLAVLSRAIIHGEPEFYHMYS------------EKSL-TWNG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 241 MLK----GLVSEyKKATVDGLKTGSTDSAGSCFTGTAELNGMRVITVVLNAKGNlhTGRFDETKKMFDYAFDNFSMKEIY 316
Cdd:PRK11397 212 ITQqnrnGLLWD-KTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSA--KGREEQARKLLRWGQQNFTTVQIL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 317 AEGDQVkGHKTISVdkGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLTAeYTGDEKdygfl 396
Cdd:PRK11397 289 HRGKKV-GTERIWY--GDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVGEIEL-YDRDKQ----- 359
|
410 420
....*....|....*....|.
gi 518542772 397 nsnLAGADLVTKENVEKANWF 417
Cdd:PRK11397 360 ---VAHWPLVTLESVGEGGMF 377
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
37-388 |
3.63e-31 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 123.43 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 37 DINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKwdqtytPDDYVyEISQDNSLSNVP----- 111
Cdd:PRK10793 43 QIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFK------ETDLV-TVGNDAWATGNPvfkgs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 112 ----LRKDGKYTVEELYQATAIYSANAAAIAIAEVVAGSETKFVEKMNAKAKELGLTDYKFvnatglenKDLHGHQPEGT 187
Cdd:PRK10793 116 slmfLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHF--------QTVHGLDADGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 188 SEdeesevSAKDMAILADHLITDYPEiletsSIAKTKFRKGTDDEMDMPNWNfmlkGLVSEyKKATVDGLKTGSTDSAGS 267
Cdd:PRK10793 188 YS------SARDMALIGQALIRDVPN-----EYAIYKEKEFTFNGIRQLNRN----GLLWD-NSLNVDGIKTGHTDKAGY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 268 CFTGTAELNGMRVITVVLNakGNLHTGRFDETKKMFDYAFDNFsmkEIYAEGDQVKGHKTISVDKGKEKEVGIVTNKAFS 347
Cdd:PRK10793 252 NLVASATEGQMRLISAVMG--GRTFKGRETESKKLLTWGFRFF---ETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVY 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518542772 348 LPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLTAEYTG 388
Cdd:PRK10793 327 LTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQLDG 367
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
310-413 |
8.54e-21 |
|
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: 86.50 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 310 FSMKEIYAEGDQVKghkTISVDKGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKETLTAPVKKGTKVGKLTaeYTGD 389
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLV--VTLD 75
|
90 100
....*....|....*....|....
gi 518542772 390 EKDygflnsnLAGADLVTKENVEK 413
Cdd:smart00936 76 GKL-------IGEVPLVALEDVEK 92
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
4-289 |
2.00e-20 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 91.28 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 4 KKCKQLLMSLVVLtLAVTCLAPMSKAK-----AASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLL 78
Cdd:PRK11669 1 MKFRVSLLSLLLL-LAGVPFAPQAVAKtaaatTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 79 EA---IDQgKVKWDQTYTPD-DYVY-------EISQDNSLSnVPLRKDGKYTVEEL-------YQAtaiysanaaaiaia 140
Cdd:PRK11669 80 DAklpLDE-KLKVDISQTPEmKGVYsrvrlnsEISRKDMLL-LALMSSENRAAASLahhypggYKA-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 141 evvagsetkFVEKMNAKAKELGLTDYKFVNATGLenkdlhghqpegtSEDEESevSAKDMAILadhLIT--DYPEILETS 218
Cdd:PRK11669 144 ---------FIKAMNAKAKALGMTNTRYVEPTGL-------------SIHNVS--TARDLTKL---LIAskQYPLIGQLS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 219 SIAK--TKFRK--------GTDDEMDMPNWNFMLKglvseykkatvdglKTGSTDSAGSCFTGTAELNGMRVITVVLNAK 288
Cdd:PRK11669 197 TTREktATFRKpnytlpfrNTNHLVYRDNWNIQLT--------------KTGFTNAAGHCLVMRTVINNRPVALVVLDAF 262
|
.
gi 518542772 289 G 289
Cdd:PRK11669 263 G 263
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
310-413 |
5.54e-19 |
|
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: 81.49 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518542772 310 FSMKEIYAEGDQVKghkTISVDKGKEKEVGIVTNKAFSLPVKNGEEKNYKAKVTLNKEtLTAPVKKGTKVGKLTAEYTGD 389
Cdd:pfam07943 1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-LEAPIKKGQVVGKLEVYLDGK 76
|
90 100
....*....|....*....|....
gi 518542772 390 ekdygflnsNLAGADLVTKENVEK 413
Cdd:pfam07943 77 ---------LIGEVPLVAKEDVEE 91
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
41-91 |
9.85e-05 |
|
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
Pssm-ID: 441286 [Multi-domain] Cd Length: 355 Bit Score: 44.29 E-value: 9.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518542772 41 SAAIMIeASSGKILYSK-------------NADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQT 91
Cdd:COG1680 34 GAAVAV-VRDGKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDDP 96
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
58-127 |
1.14e-04 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 43.73 E-value: 1.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518542772 58 NADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQ--TYTPDDYVyeisqDNSLSNVPLRKDGKYTVEELYQAT 127
Cdd:COG2367 51 NADERFPAASTFKLPVLAAVLRQVDAGKLSLDErvTLTPEDLV-----GGSGILQKLPDGTGLTLRELAELM 117
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
55-123 |
1.21e-04 |
|
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: 43.03 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518542772 55 YSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQ--TYTPDDYVyeisqDNSLSNVPLRKDGKYTVEEL 123
Cdd:pfam13354 13 LGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDErlTVTAEDKV-----GGSGILQYLPDGSQLSLRDL 78
|
|
| |
