|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
1-400 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 804.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 1 MTHDAFSLRGLAAGCALLLLVAPAVQAADQLPDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQAL 80
Cdd:PRK10001 1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 81 KAGKIKLTDTVTVGRDAWATGNPALRGSSVMFLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQ 160
Cdd:PRK10001 81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 161 KIGLTNTTFKTVHGLDAPGQFSTARDMALLTKAMIHDVPEEYAVHKEKEFTFNKIRQPNRNRLLWSTNLNADGVKTGTTA 240
Cdd:PRK10001 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 241 GAGYNLVSSATQGDMRLIAVVLGTKTDRIRFNESEKLLTWGFRFYETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSV 320
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 321 TIPRGQLKNLKASYNLTEPQLTAPLAKGQVVGTIDFKLNDKTIEQRPLIVMEDVKEGGFFSRIVDFVLMKLHGWFGSWFS 400
Cdd:PRK10001 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWFS 400
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
24-382 |
5.26e-143 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 409.61 E-value: 5.26e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 24 AVQAADQLPDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGnp 103
Cdd:COG1686 13 LAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 104 alrgSSVMFLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLDAPGQFST 183
Cdd:COG1686 91 ----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYST 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 184 ARDMALLTKAMIHDVPEEYAVHKEKEFTFN---KIRQPNRNRLLWSTNlNADGVKTGTTAGAGYNLVSSATQGDMRLIAV 260
Cdd:COG1686 167 ARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGYTDAAGYCLVASAKRGGRRLIAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 261 VLGTKTDRIRFNESEKLLTWGFrfyetvtpikpdatfisqrvwfgdsnevklgageagsvtiPRGQlkNLKASYNLTEPq 340
Cdd:COG1686 246 VLGAPSEKARFADAAKLLDYGF----------------------------------------PKGE--ALKAEVVLDGP- 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 505807087 341 LTAPLAKGQVVGTIDFKLNDKTIEQRPLIVMEDVKEGGFFSR 382
Cdd:COG1686 283 LKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
32-265 |
8.58e-123 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 354.77 E-value: 8.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 32 PDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGNPalrGSSVM 111
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 112 FLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLDAPGQFSTARDMALLT 191
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807087 192 KAMIHDVPEEYAVHKEKEFTF---NKIRQPNRNRLLWSTNLNADGVKTGTTAGAGYNLVSSATQGDMRLIAVVLGTK 265
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
285-376 |
5.58e-31 |
|
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.
Pssm-ID: 198004 [Multi-domain] Cd Length: 92 Bit Score: 113.47 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 285 YETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSVTIPRGQLKNLKASYNLTEPQLTAPLAKGQVVGTIDFKLNDKTIE 364
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 505807087 365 QRPLIVMEDVKE 376
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
1-400 |
0e+00 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 804.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 1 MTHDAFSLRGLAAGCALLLLVAPAVQAADQLPDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQAL 80
Cdd:PRK10001 1 MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 81 KAGKIKLTDTVTVGRDAWATGNPALRGSSVMFLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQ 160
Cdd:PRK10001 81 KADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 161 KIGLTNTTFKTVHGLDAPGQFSTARDMALLTKAMIHDVPEEYAVHKEKEFTFNKIRQPNRNRLLWSTNLNADGVKTGTTA 240
Cdd:PRK10001 161 KLGLTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 241 GAGYNLVSSATQGDMRLIAVVLGTKTDRIRFNESEKLLTWGFRFYETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSV 320
Cdd:PRK10001 241 GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 321 TIPRGQLKNLKASYNLTEPQLTAPLAKGQVVGTIDFKLNDKTIEQRPLIVMEDVKEGGFFSRIVDFVLMKLHGWFGSWFS 400
Cdd:PRK10001 321 TIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWFGSWFS 400
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
31-396 |
0e+00 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 568.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 31 LPDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGNPALRGSSV 110
Cdd:PRK10793 38 IPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATGNPVFKGSSL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 111 MFLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLDAPGQFSTARDMALL 190
Cdd:PRK10793 118 MFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 191 TKAMIHDVPEEYAVHKEKEFTFNKIRQPNRNRLLWSTNLNADGVKTGTTAGAGYNLVSSATQGDMRLIAVVLGTKTDRIR 270
Cdd:PRK10793 198 GQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 271 FNESEKLLTWGFRFYETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSVTIPRGQLKNLKASYNLTEPQLTAPLAKGQV 350
Cdd:PRK10793 278 ETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTSELHAPLQKNQV 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 505807087 351 VGTIDFKLNDKTIEQRPLIVMEDVKEGGFFSRIVDFVLMKLHGWFG 396
Cdd:PRK10793 358 VGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG 403
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
24-391 |
7.99e-158 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 449.66 E-value: 7.99e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 24 AVQAADQLPDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGNP 103
Cdd:PRK11397 21 AAENIPFSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 104 ALRGSSVMFLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLDAPGQFST 183
Cdd:PRK11397 101 VFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGLDAPGQHSS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 184 ARDMALLTKAMIHDVPEEYAVHKEKEFTFNKIRQPNRNRLLWSTNLNADGVKTGTTAGAGYNLVSSATQGDMRLIAVVLG 263
Cdd:PRK11397 181 AYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 264 TKTDRIRFNESEKLLTWGFRFYETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSVTIPRGQLKNLKASYNLTEPQLTA 343
Cdd:PRK11397 261 ADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEA 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 505807087 344 PLAKGQVVGTIDFKLNDKTIEQRPLIVMEDVKEGGFFSRIVDFVLMKL 391
Cdd:PRK11397 341 PISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGGMFSRLSDYFHHKA 388
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
24-382 |
5.26e-143 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 409.61 E-value: 5.26e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 24 AVQAADQLPDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGnp 103
Cdd:COG1686 13 LAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 104 alrgSSVMFLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLDAPGQFST 183
Cdd:COG1686 91 ----GSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDPGHYST 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 184 ARDMALLTKAMIHDVPEEYAVHKEKEFTFN---KIRQPNRNRLLWSTNlNADGVKTGTTAGAGYNLVSSATQGDMRLIAV 260
Cdd:COG1686 167 ARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLGRYP-GVDGLKTGYTDAAGYCLVASAKRGGRRLIAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 261 VLGTKTDRIRFNESEKLLTWGFrfyetvtpikpdatfisqrvwfgdsnevklgageagsvtiPRGQlkNLKASYNLTEPq 340
Cdd:COG1686 246 VLGAPSEKARFADAAKLLDYGF----------------------------------------PKGE--ALKAEVVLDGP- 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 505807087 341 LTAPLAKGQVVGTIDFKLNDKTIEQRPLIVMEDVKEGGFFSR 382
Cdd:COG1686 283 LKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
32-265 |
8.58e-123 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 354.77 E-value: 8.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 32 PDAPSIDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGNPalrGSSVM 111
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNP---GSSNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 112 FLKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLDAPGQFSTARDMALLT 191
Cdd:pfam00768 78 FLKPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807087 192 KAMIHDVPEEYAVHKEKEFTF---NKIRQPNRNRLLWSTNLNADGVKTGTTAGAGYNLVSSATQGDMRLIAVVLGTK 265
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
285-376 |
5.58e-31 |
|
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.
Pssm-ID: 198004 [Multi-domain] Cd Length: 92 Bit Score: 113.47 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 285 YETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSVTIPRGQLKNLKASYNLTEPQLTAPLAKGQVVGTIDFKLNDKTIE 364
Cdd:smart00936 1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVTLDGKLIG 80
|
90
....*....|..
gi 505807087 365 QRPLIVMEDVKE 376
Cdd:smart00936 81 EVPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
285-376 |
9.46e-29 |
|
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: 107.68 E-value: 9.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 285 YETVTPIKPDATFISQRVWFGDSNEVKLGAGEAGSVTIPRGQLKNLKASYNLTEPqLTAPLAKGQVVGTIDFKLNDKTIE 364
Cdd:pfam07943 1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP-LEAPIKKGQVVGKLEVYLDGKLIG 79
|
90
....*....|..
gi 505807087 365 QRPLIVMEDVKE 376
Cdd:pfam07943 80 EVPLVAKEDVEE 91
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
23-295 |
1.62e-17 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 82.42 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 23 PAVQAADQLPDAPS----IDARAWILMDYASGKVLSEGNADEKLDPASLTKIMTSYVVGQAlkagKIKLTDTVTVGrdaw 98
Cdd:PRK11669 21 PQAVAKTAAATTASqpqeIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPLDEKLKVD---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 99 ATGNPALRG--SSVmflKPGMQVSVEDLNKGVIIQSGNDASIAIADYVAGSQDSFVNLMNGYAQKIGLTNTTFKTVHGLd 176
Cdd:PRK11669 93 ISQTPEMKGvySRV---RLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPTGL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 177 APGQFSTARDMALLTKAMiHDVP--EEYAVHKEKEFTFnkiRQP-------NRNRLLWSTNLNADGVKTGTTAGAGYNLV 247
Cdd:PRK11669 169 SIHNVSTARDLTKLLIAS-KQYPliGQLSTTREKTATF---RKPnytlpfrNTNHLVYRDNWNIQLTKTGFTNAAGHCLV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 505807087 248 SSaTQGDMRLIA-VVLGTKTDRIRFNESEKLLTWgfrfYET--VTPIKPDA 295
Cdd:PRK11669 245 MR-TVINNRPVAlVVLDAFGKYTHFADASRLRTW----IETgkVTPVPAAA 290
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
44-197 |
8.15e-13 |
|
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: 66.91 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 44 LMDYASGKVLSEgNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGNPALRgssvmFLKPGMQVSVED 123
Cdd:pfam13354 4 VRDLDTGEELGI-NGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQ-----YLPDGSQLSLRD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807087 124 LNKGVIIQSGNDASIAIADYVAGSQdsfvnlMNGYAQKIGLTNTTF----KTVHGLDAPGQ-FSTARDMALLTKAMIHD 197
Cdd:pfam13354 78 LLTLMIAVSDNTATNLLIDRLGLEA------VNARLRALGLRDTRLrrklPDLRAADKGGTnTTTARDMAKLLEALYRG 150
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
38-190 |
4.41e-10 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 59.91 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807087 38 DARAWI-LMDYASGKVLSEgNADEKLDPASLTKIMTSYVVGQALKAGKIKLTDTVTVGRDAWATGNPALRgssvmFLKPG 116
Cdd:COG2367 32 GGRVGVyVLDLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGILQ-----KLPDG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807087 117 MQVSVEDLNKGVIIQSGNDASIAIADYVAGSQdsfvnlMNGYAQKIGLTNTTF--KTVHGLDAPGQF---STARDMALL 190
Cdd:COG2367 106 TGLTLRELAELMITVSDNTATNLLLRLLGPDA------VNAFLRSLGLTDTRLdrKEPDLNELPGDGrntTTPRDMARL 178
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
65-92 |
6.13e-03 |
|
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
Pssm-ID: 441286 [Multi-domain] Cd Length: 355 Bit Score: 38.51 E-value: 6.13e-03
10 20
....*....|....*....|....*...
gi 505807087 65 ASLTKIMTSYVVGQALKAGKIKLTDTVT 92
Cdd:COG1680 71 ASVTKSFTATAVLQLVEEGKLDLDDPVS 98
|
|
|