|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-367 |
2.49e-114 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 336.04 E-value: 2.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 1 MKRskksiIYLFIVLLCLSGWPSISSAAGSVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAIL---AIESGKI- 76
Cdd:COG1686 1 MKK-----LLLLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVvleALKAGKIs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 77 -NKTVTVSHNAVGVEGSSVYLVEGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNP 155
Cdd:COG1686 76 lDDKVTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 156 HGLDDhENHRSTAHDMALLMRYAMNN-KIFKEISGTKVYRMKHPeekWDRVWKNKNKLLTTlYAYCTGGKTGYTKLAKRT 234
Cdd:COG1686 156 TGLPD-PGHYSTARDLALLARAAIKDyPEFYEIFSTKEFTFPNG---RGITLRNTNRLLGR-YPGVDGLKTGYTDAAGYC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 235 LVTTATKDGMDLIAVTINAPDD---WNDHISMYENAFDkydmtslaakgeladiKDSFYKDQLYIKRNVVYPLTKKEqss 311
Cdd:COG1686 231 LVASAKRGGRRLIAVVLGAPSEkarFADAAKLLDYGFP----------------KGEALKAEVVLDGPLKAPVKKGQ--- 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2021574318 312 vevkttliqpkkqwketgevpnVVGKLDIYRSGETIDSVPIYfEKQSEQQKGFFDR 367
Cdd:COG1686 292 ----------------------VVGTLVVTLDGKTIAEVPLV-AAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
26-254 |
3.44e-80 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 245.76 E-value: 3.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 26 SAAGSVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAILAIESGKINK-----TVTVSHNAVGVEG---SSVYLV 97
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKikeddMVTISEDAWATGNpgsSNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 98 EGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNPHGLDDHENHrSTAHDMALLMRY 177
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQY-SSARDMAILAKA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021574318 178 AmnnkIFKEISGTKVYRMKHPEEKWDR--VWKNKNKLLTTLYAYCTGGKTGYTKLAKRTLVTTATKDGMDLIAVTINAP 254
Cdd:pfam00768 160 L----IKDLPEELSITKEKSFTFRGINkiNQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
27-368 |
1.84e-43 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 155.54 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 27 AAGSVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAIL---AIESGKINKT--VTVSHNA-----VGVEGSSV-Y 95
Cdd:PRK10001 33 EAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVvgqALKADKIKLTdmVTVGKDAwatgnPALRGSSVmF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 96 LVEGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNPHGLdDHENHRSTAHDMALLM 175
Cdd:PRK10001 113 LKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL-DAPGQFSTARDMALLG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 176 R---------YAMNNKifKEISGTKVyrmKHPeekwdrvwkNKNKLLTTLYAYCTGGKTGYTKLAKRTLVTTATKDGMDL 246
Cdd:PRK10001 192 KalihdvpeeYAIHKE--KEFTFNKI---RQP---------NRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 247 IAVTINAPDD---WNDHISMYENAFDKYDMTSLAAKGELADIKDSFYKDQLYIKR------NVVYPltKKEQSSVEVKTT 317
Cdd:PRK10001 258 ISVVLGAKTDrirFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLgageagSVTIP--RGQLKNLKASYT 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2021574318 318 LIQPkkQWKETGEVPNVVGKLDIYRSGETIDSVPIYFeKQSEQQKGFFDRV 368
Cdd:PRK10001 336 LTEP--QLTAPLKKGQVVGTIDFQLNGKSIEQRPLIV-MENVEEGGFFSRM 383
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
271-353 |
2.86e-04 |
|
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: 39.51 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 271 YDMTSLAAKGE-LADIKDSFYKD---QLYIKRNVVYPLTKKEQSSVEVKTTLIQPKKQWK-ETGEVpnvVGKLDIYRSGE 345
Cdd:smart00936 1 FETVKLYKKGQvVGTVKVWKGKEktvKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPiKKGQV---VGTLVVTLDGK 77
|
....*...
gi 2021574318 346 TIDSVPIY 353
Cdd:smart00936 78 LIGEVPLV 85
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
1-367 |
2.49e-114 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 336.04 E-value: 2.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 1 MKRskksiIYLFIVLLCLSGWPSISSAAGSVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAIL---AIESGKI- 76
Cdd:COG1686 1 MKK-----LLLLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVvleALKAGKIs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 77 -NKTVTVSHNAVGVEGSSVYLVEGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNP 155
Cdd:COG1686 76 lDDKVTVSEEAARTGGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 156 HGLDDhENHRSTAHDMALLMRYAMNN-KIFKEISGTKVYRMKHPeekWDRVWKNKNKLLTTlYAYCTGGKTGYTKLAKRT 234
Cdd:COG1686 156 TGLPD-PGHYSTARDLALLARAAIKDyPEFYEIFSTKEFTFPNG---RGITLRNTNRLLGR-YPGVDGLKTGYTDAAGYC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 235 LVTTATKDGMDLIAVTINAPDD---WNDHISMYENAFDkydmtslaakgeladiKDSFYKDQLYIKRNVVYPLTKKEqss 311
Cdd:COG1686 231 LVASAKRGGRRLIAVVLGAPSEkarFADAAKLLDYGFP----------------KGEALKAEVVLDGPLKAPVKKGQ--- 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2021574318 312 vevkttliqpkkqwketgevpnVVGKLDIYRSGETIDSVPIYfEKQSEQQKGFFDR 367
Cdd:COG1686 292 ----------------------VVGTLVVTLDGKTIAEVPLV-AAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
26-254 |
3.44e-80 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 245.76 E-value: 3.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 26 SAAGSVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAILAIESGKINK-----TVTVSHNAVGVEG---SSVYLV 97
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKikeddMVTISEDAWATGNpgsSNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 98 EGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNPHGLDDHENHrSTAHDMALLMRY 177
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQY-SSARDMAILAKA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021574318 178 AmnnkIFKEISGTKVYRMKHPEEKWDR--VWKNKNKLLTTLYAYCTGGKTGYTKLAKRTLVTTATKDGMDLIAVTINAP 254
Cdd:pfam00768 160 L----IKDLPEELSITKEKSFTFRGINkiNQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
27-368 |
1.84e-43 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 155.54 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 27 AAGSVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAIL---AIESGKINKT--VTVSHNA-----VGVEGSSV-Y 95
Cdd:PRK10001 33 EAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVvgqALKADKIKLTdmVTVGKDAwatgnPALRGSSVmF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 96 LVEGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNPHGLdDHENHRSTAHDMALLM 175
Cdd:PRK10001 113 LKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL-DAPGQFSTARDMALLG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 176 R---------YAMNNKifKEISGTKVyrmKHPeekwdrvwkNKNKLLTTLYAYCTGGKTGYTKLAKRTLVTTATKDGMDL 246
Cdd:PRK10001 192 KalihdvpeeYAIHKE--KEFTFNKI---RQP---------NRNRLLWSSNLNVDGMKTGTTAGAGYNLVASATQGDMRL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 247 IAVTINAPDD---WNDHISMYENAFDKYDMTSLAAKGELADIKDSFYKDQLYIKR------NVVYPltKKEQSSVEVKTT 317
Cdd:PRK10001 258 ISVVLGAKTDrirFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLgageagSVTIP--RGQLKNLKASYT 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2021574318 318 LIQPkkQWKETGEVPNVVGKLDIYRSGETIDSVPIYFeKQSEQQKGFFDRV 368
Cdd:PRK10001 336 LTEP--QLTAPLKKGQVVGTIDFQLNGKSIEQRPLIV-MENVEEGGFFSRM 383
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
1-253 |
6.56e-36 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 134.95 E-value: 6.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 1 MKRskksiiYLFIVLLCLsgWPSISSAAG-----------SVSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAIL 69
Cdd:PRK11397 1 LKR------RLIIAASLF--AFNLSSAFAaenipfspqppAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 70 ---AIESGKI--NKTVTVSHNAVG-----VEGSSV-YLVEGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLM 138
Cdd:PRK11397 73 vdrAIDSHRItpDDIVTVGRDAWAkdnpvFVGSSLmFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 139 NKKAEEIGMTNTTFQNPHGLDDHENHrSTAHDMALLMRYAmnnkifkeISGT-KVYRMKhpEEK---WDRV-WKNKNKLL 213
Cdd:PRK11397 153 NNYVEKLHLKDTHFETVHGLDAPGQH-SSAYDLAVLSRAI--------IHGEpEFYHMY--SEKsltWNGItQQNRNGLL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2021574318 214 TTLYAYCTGGKTGYTKLAKRTLVTTATKDGMDLIAVTINA 253
Cdd:PRK11397 222 WDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGA 261
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
31-254 |
5.28e-33 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 127.28 E-value: 5.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 31 VSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAIL---AIESGKI--NKTVTVSHNAVGV-----EGSSV-YLVEG 99
Cdd:PRK10793 44 IDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVigqAMKAGKFkeTDLVTVGNDAWATgnpvfKGSSLmFLKPG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 100 EKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNTTFQNPHGLdDHENHRSTAHDMALLMRyAM 179
Cdd:PRK10793 124 MQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGL-DADGQYSSARDMALIGQ-AL 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2021574318 180 NNKIFKEISgtkVYRMKhpEEKWDRVWK-NKNKLLTTLYAYCTGGKTGYTKLAKRTLVTTATKDGMDLIAVTINAP 254
Cdd:PRK10793 202 IRDVPNEYA---IYKEK--EFTFNGIRQlNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 272
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
11-236 |
5.12e-23 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 97.83 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 11 LFIVLLCLSGWPSISSAAGS------------VSAHSAILMEQKSGRVLYAKNADQVSRIASITKIMTAILAIESG---- 74
Cdd:PRK11669 7 LLSLLLLLAGVPFAPQAVAKtaaattasqpqeIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDAKlpld 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 75 -KInkTVTVSHNAV--GVEgSSVYLveGEKIKLKD-LVYGLMlRSGNDAAVAIAEAVGGSEDGFVYLMNKKAEEIGMTNT 150
Cdd:PRK11669 87 eKL--KVDISQTPEmkGVY-SRVRL--NSEISRKDmLLLALM-SSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 151 TFQNPHGLDDHenHRSTAHDMALLMRYAMNNKIFKEISGT--KVYRMKHPEEKWDrvWKNKNKL---------LTtlyay 219
Cdd:PRK11669 161 RYVEPTGLSIH--NVSTARDLTKLLIASKQYPLIGQLSTTreKTATFRKPNYTLP--FRNTNHLvyrdnwniqLT----- 231
|
250
....*....|....*..
gi 2021574318 220 ctggKTGYTKLAKRTLV 236
Cdd:PRK11669 232 ----KTGFTNAAGHCLV 244
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
11-176 |
3.63e-09 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 57.22 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 11 LFIVLLCLSGWPSISSAAGSVSAhsaiLMEQKSGRV-LYAK----------NADQVSRIASITK--IMTAIL-AIESGKI 76
Cdd:COG2367 4 LALLLLAAAAAAPASALEAELAA----LEAALGGRVgVYVLdldtgetvgiNADERFPAASTFKlpVLAAVLrQVDAGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 77 --NKTVTVShNAVGVEGSSV--YLVEGEKIKLKDLVYGLMLRSGNDAAVAIAEAVGGSEdgfvylMNKKAEEIGMTNTTF 152
Cdd:COG2367 80 slDERVTLT-PEDLVGGSGIlqKLPDGTGLTLRELAELMITVSDNTATNLLLRLLGPDA------VNAFLRSLGLTDTRL 152
|
170 180
....*....|....*....|....*...
gi 2021574318 153 QN----PHGLDDHENHRSTAHDMALLMR 176
Cdd:COG2367 153 DRkepdLNELPGDGRNTTTPRDMARLLA 180
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
51-176 |
4.46e-07 |
|
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: 49.97 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 51 NADQVSRIASITKIMTAILA---IESGKIN--KTVTVSHNAVgVEGSSV--YLVEGEKIKLKDLVYGLMLRSGNDAAVAI 123
Cdd:pfam13354 16 NGDRSFPAASTIKVPILLAVleqVDEGKLSldERLTVTAEDK-VGGSGIlqYLPDGSQLSLRDLLTLMIAVSDNTATNLL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2021574318 124 AEAVGGSEdgfvylMNKKAEEIGMTNTTFQN----PHGLDDHENHRSTAHDMALLMR 176
Cdd:pfam13354 95 IDRLGLEA------VNARLRALGLRDTRLRRklpdLRAADKGGTNTTTARDMAKLLE 145
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
271-353 |
1.35e-04 |
|
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: 40.27 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 271 YDMTSLAAKGELADIKDSFYKDQ----LYIKRNVVYPLTKKEQSSVEVKTTLiqpKKQWKETGEVPNVVGKLDIYRSGET 346
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKktvpLGAKEDVYVTVPKGEKKKLKAKVTL---KKPLEAPIKKGQVVGKLEVYLDGKL 77
|
....*..
gi 2021574318 347 IDSVPIY 353
Cdd:pfam07943 78 IGEVPLV 84
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
271-353 |
2.86e-04 |
|
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: 39.51 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021574318 271 YDMTSLAAKGE-LADIKDSFYKD---QLYIKRNVVYPLTKKEQSSVEVKTTLIQPKKQWK-ETGEVpnvVGKLDIYRSGE 345
Cdd:smart00936 1 FETVKLYKKGQvVGTVKVWKGKEktvKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPiKKGQV---VGTLVVTLDGK 77
|
....*...
gi 2021574318 346 TIDSVPIY 353
Cdd:smart00936 78 LIGEVPLV 85
|
|
| |
