|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
62-448 |
2.23e-115 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 341.82 E-value: 2.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 62 ASAVKATKESLKLEVTSAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLTRGSR 141
Cdd:COG1686 14 AAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGGSK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 142 IFLAEGDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLgreDMPekfrpegtd 221
Cdd:COG1686 94 MGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGL---PDP--------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 222 ETVMSAMDVAKLVRAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLeankdipnfkrYAYPGLDGMKTGFTNEAGNC 301
Cdd:COG1686 162 GHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNGRGITLRNTNRLL-----------GRYPGVDGLKTGYTDAAGYC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 302 FAGTAERDGMRLISVVMGTDinDKGKRFVETAKLLDHGYnnyevqpvvapkqavdgvaaapikkgvstevpvvpengvnf 381
Cdd:COG1686 231 LVASAKRGGRRLIAVVLGAP--SEKARFADAAKLLDYGF----------------------------------------- 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2189018674 382 vvPKGASTegkithEVKLTPANELIAPIKNGQKIGTITFTYKDNGLeqkKTVNLIASEEVEKGSWWR 448
Cdd:COG1686 268 --PKGEAL------KAEVVLDGPLKAPVKKGQVVGTLVVTLDGKTI---AEVPLVAAEDVEKAGFFS 323
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
78-321 |
9.92e-69 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 219.18 E-value: 9.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 78 SAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLTRG---SRIFLAEGDKHTVRD 154
Cdd:pfam00768 10 SAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLKPGSQVSVKD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 155 LYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLGREDMpekfrpegtdetVMSAMDVAKLV 234
Cdd:pfam00768 90 LLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQ------------YSSARDMAILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 235 RAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLeankdipnfkRYAYPGLDGMKTGFTNEAGNCFAGTAERDGMRLI 314
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFRGINKINQRNRNGLL----------WDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLI 227
|
....*..
gi 2189018674 315 SVVMGTD 321
Cdd:pfam00768 228 SVVMGAF 234
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
61-457 |
3.91e-48 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 170.17 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 61 SASAVKATKESLKLEVTSAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLT--- 137
Cdd:PRK10001 24 TAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATgnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 138 --RGSRI-FLAEGDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLgreDMPEK 214
Cdd:PRK10001 104 alRGSSVmFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL---DAPGQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 215 FRpegtdetvmSAMDVAKLVRAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLEANkdipnfkryaypgLDGMKTGF 294
Cdd:PRK10001 181 FS---------TARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLN-------------VDGMKTGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 295 TNEAGNCFAGTAERDGMRLISVVMGTDINdkGKRFVETAKLLDHGYNNYEvqpVVAPKQAVDGVAAAPIKKGVSTEVPVV 374
Cdd:PRK10001 239 TAGAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGFRFFE---TVTPIKPDATFVTQRVWFGDKSEVNLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 375 PENGVNFVVPKGASTEGKITHEVKltpANELIAPIKNGQKIGTITFTYKDNGLEQKKtvnLIASEEVEKGSwwrlFFRAI 454
Cdd:PRK10001 314 AGEAGSVTIPRGQLKNLKASYTLT---EPQLTAPLKKGQVVGTIDFQLNGKSIEQRP---LIVMENVEEGG----FFSRM 383
|
...
gi 2189018674 455 GEF 457
Cdd:PRK10001 384 WDF 386
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
71-349 |
2.20e-41 |
|
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: 151.28 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 71 SLKLEVTSAILMeASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVT-TSEHASLTRG---SRIFLAE 146
Cdd:NF038258 35 SEQYNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKiTSDYEKMSTLpnlSTFPLKP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 147 GDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTG----LGREDMPEKFRPEGTde 222
Cdd:NF038258 114 GQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGadnnLLKPYAPKKYKDETK-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 223 TVMSAMDVAKLVRAIVIKHPEFRDFTtiqeykfreRDETPIQ------NLNWMLEANKDipnfkryAYPGLDGMKTGFTN 296
Cdd:NF038258 192 SKSTAKDMAILSQHLIKKHPKILKYT---------KLTADTQhgvtlyTTNLSLPGQPM-------SLKGTDGLKTGTSD 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2189018674 297 EAGNcFAGTAERDGMRLISVVMG-TDINDKGKRFVE---TAKLLDHGYNNYEVQPVV 349
Cdd:NF038258 256 EGYN-LALTTKRDGLRINQVIMNvGPYPSEGAKHARnkiANALMERAFKQYEYKKVL 311
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
343-443 |
7.03e-13 |
|
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: 64.16 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 343 YEVQPVVAPKQAVdgvAAAPIKKGVSTEVPVVPENGVNFVVPKGasTEGKITHEVKLtPANELIAPIKNGQKIGTItfTY 422
Cdd:smart00936 1 FETVKLYKKGQVV---GTVKVWKGKEKTVKLGAKEDVYVTLPKG--EKKKLKAKVVL-DKPELEAPIKKGQVVGTL--VV 72
|
90 100
....*....|....*....|.
gi 2189018674 423 KDNGlEQKKTVNLIASEEVEK 443
Cdd:smart00936 73 TLDG-KLIGEVPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
62-448 |
2.23e-115 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 341.82 E-value: 2.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 62 ASAVKATKESLKLEVTSAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLTRGSR 141
Cdd:COG1686 14 AAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAARTGGSK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 142 IFLAEGDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLgreDMPekfrpegtd 221
Cdd:COG1686 94 MGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGL---PDP--------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 222 ETVMSAMDVAKLVRAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLeankdipnfkrYAYPGLDGMKTGFTNEAGNC 301
Cdd:COG1686 162 GHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNGRGITLRNTNRLL-----------GRYPGVDGLKTGYTDAAGYC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 302 FAGTAERDGMRLISVVMGTDinDKGKRFVETAKLLDHGYnnyevqpvvapkqavdgvaaapikkgvstevpvvpengvnf 381
Cdd:COG1686 231 LVASAKRGGRRLIAVVLGAP--SEKARFADAAKLLDYGF----------------------------------------- 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2189018674 382 vvPKGASTegkithEVKLTPANELIAPIKNGQKIGTITFTYKDNGLeqkKTVNLIASEEVEKGSWWR 448
Cdd:COG1686 268 --PKGEAL------KAEVVLDGPLKAPVKKGQVVGTLVVTLDGKTI---AEVPLVAAEDVEKAGFFS 323
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
78-321 |
9.92e-69 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 219.18 E-value: 9.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 78 SAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLTRG---SRIFLAEGDKHTVRD 154
Cdd:pfam00768 10 SAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNpgsSNIFLKPGSQVSVKD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 155 LYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLGREDMpekfrpegtdetVMSAMDVAKLV 234
Cdd:pfam00768 90 LLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQ------------YSSARDMAILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 235 RAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLeankdipnfkRYAYPGLDGMKTGFTNEAGNCFAGTAERDGMRLI 314
Cdd:pfam00768 158 KALIKDLPEELSITKEKSFTFRGINKINQRNRNGLL----------WDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLI 227
|
....*..
gi 2189018674 315 SVVMGTD 321
Cdd:pfam00768 228 SVVMGAF 234
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
61-457 |
3.91e-48 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 170.17 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 61 SASAVKATKESLKLEVTSAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLT--- 137
Cdd:PRK10001 24 TAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATgnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 138 --RGSRI-FLAEGDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLgreDMPEK 214
Cdd:PRK10001 104 alRGSSVmFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL---DAPGQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 215 FRpegtdetvmSAMDVAKLVRAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLEANkdipnfkryaypgLDGMKTGF 294
Cdd:PRK10001 181 FS---------TARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLN-------------VDGMKTGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 295 TNEAGNCFAGTAERDGMRLISVVMGTDINdkGKRFVETAKLLDHGYNNYEvqpVVAPKQAVDGVAAAPIKKGVSTEVPVV 374
Cdd:PRK10001 239 TAGAGYNLVASATQGDMRLISVVLGAKTD--RIRFNESEKLLTWGFRFFE---TVTPIKPDATFVTQRVWFGDKSEVNLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 375 PENGVNFVVPKGASTEGKITHEVKltpANELIAPIKNGQKIGTITFTYKDNGLEQKKtvnLIASEEVEKGSwwrlFFRAI 454
Cdd:PRK10001 314 AGEAGSVTIPRGQLKNLKASYTLT---EPQLTAPLKKGQVVGTIDFQLNGKSIEQRP---LIVMENVEEGG----FFSRM 383
|
...
gi 2189018674 455 GEF 457
Cdd:PRK10001 384 WDF 386
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
78-445 |
5.38e-43 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 156.13 E-value: 5.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 78 SAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHA-----SLTRGSRI-FLAEGDKHT 151
Cdd:PRK11397 38 SWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAwakdnPVFVGSSLmFLKEGDRVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 152 VRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLgreDMPEKFRpegtdetvmSAMDVA 231
Cdd:PRK11397 118 VRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGL---DAPGQHS---------SAYDLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 232 KLVRAIVIKHPEFRdfttiqeYKFRERDET----PIQNLNWMLeANKDIpnfkryaypGLDGMKTGFTNEAG-NCFAGTA 306
Cdd:PRK11397 186 VLSRAIIHGEPEFY-------HMYSEKSLTwngiTQQNRNGLL-WDKTM---------NVDGLKTGHTSGAGfNLIASAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 307 erDGM-RLISVVMGTDiNDKGkRFVETAKLLDHGYNNYE-VQPVVAPKQavdgVAAAPIKKGVSTEVPVVPENGVNFVVP 384
Cdd:PRK11397 249 --DGQrRLIAVVMGAD-SAKG-REEQARKLLRWGQQNFTtVQILHRGKK----VGTERIWYGDKENIALGTEQDFWMVLP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2189018674 385 KG--ASTEGKITHEVKltpanELIAPIKNGQKIGTITFTYKDnglEQKKTVNLIASEEVEKGS 445
Cdd:PRK11397 321 KAeiPHIKAKYVLDGK-----ELEAPISAHQRVGEIELYDRD---KQVAHWPLVTLESVGEGG 375
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
71-349 |
2.20e-41 |
|
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: 151.28 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 71 SLKLEVTSAILMeASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVT-TSEHASLTRG---SRIFLAE 146
Cdd:NF038258 35 SEQYNPEGAIVT-TQTGQILYDYHGNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKiTSDYEKMSTLpnlSTFPLKP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 147 GDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTG----LGREDMPEKFRPEGTde 222
Cdd:NF038258 114 GQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGadnnLLKPYAPKKYKDETK-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 223 TVMSAMDVAKLVRAIVIKHPEFRDFTtiqeykfreRDETPIQ------NLNWMLEANKDipnfkryAYPGLDGMKTGFTN 296
Cdd:NF038258 192 SKSTAKDMAILSQHLIKKHPKILKYT---------KLTADTQhgvtlyTTNLSLPGQPM-------SLKGTDGLKTGTSD 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2189018674 297 EAGNcFAGTAERDGMRLISVVMG-TDINDKGKRFVE---TAKLLDHGYNNYEVQPVV 349
Cdd:NF038258 256 EGYN-LALTTKRDGLRINQVIMNvGPYPSEGAKHARnkiANALMERAFKQYEYKKVL 311
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
73-469 |
2.86e-40 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 149.23 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 73 KLEVTSAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEHASLT-----RGSRI-FLAE 146
Cdd:PRK10793 43 QIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWATgnpvfKGSSLmFLKP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 147 GDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLgreDMPEKFRpegtdetvmS 226
Cdd:PRK10793 123 GMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGL---DADGQYS---------S 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 227 AMDVAKLVRAIVIKHPEFRDFTTIQEYKFRERDETPIQNLNWMLEANkdipnfkryaypgLDGMKTGFTNEAGNCFAGTA 306
Cdd:PRK10793 191 ARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLN-------------VDGIKTGHTDKAGYNLVASA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 307 ERDGMRLISVVMGTDiNDKGkRFVETAKLLDHGYNNYEvqpVVAPKQAVDGVAAAPIKKGVSTEVPVVPENGVNFVVPKG 386
Cdd:PRK10793 258 TEGQMRLISAVMGGR-TFKG-RETESKKLLTWGFRFFE---TVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 387 ASTEGKITHEVKLTpanELIAPIKNGQKIGTITFTYKDNGLEQKKtvnLIASEEVEKGSwwrlffraigeFFVDLFQSIK 466
Cdd:PRK10793 333 RMKDLKASYVLNTS---ELHAPLQKNQVVGTINFQLDGKTIEQRP---LVVLQEIPEGN-----------FFGKIIDYIK 395
|
...
gi 2189018674 467 NLF 469
Cdd:PRK10793 396 LMF 398
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
61-330 |
1.50e-17 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 83.19 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 61 SASAVKATKESLKLEVTSAILMEASTGQVLVNIDSNTPKPPASMTKMMTEYIVMEkvknGELSWEEEVT-TSEHASLTRG 139
Cdd:PRK11669 26 KTAAATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLD----AKLPLDEKLKvDISQTPEMKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 140 --SRIFLaeGDKHTVRDLYIAMAIGSANDATVALAERIAGTEKEFANLMNETAKKLGMTTAHFINSTGLGREDmpekfrp 217
Cdd:PRK11669 102 vySRVRL--NSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPTGLSIHN------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 218 egtdetVMSAMDVAKLVRAiVIKHPEFRDFTTIQE--YKFRERDET-PIQNLNWMLeaNKDIPNFKRyaypgldgMKTGF 294
Cdd:PRK11669 173 ------VSTARDLTKLLIA-SKQYPLIGQLSTTREktATFRKPNYTlPFRNTNHLV--YRDNWNIQL--------TKTGF 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 2189018674 295 TNEAGNCfagtaerdgmrlisVVMGTDINDKGKRFV 330
Cdd:PRK11669 236 TNAAGHC--------------LVMRTVINNRPVALV 257
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
343-443 |
7.03e-13 |
|
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: 64.16 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 343 YEVQPVVAPKQAVdgvAAAPIKKGVSTEVPVVPENGVNFVVPKGasTEGKITHEVKLtPANELIAPIKNGQKIGTItfTY 422
Cdd:smart00936 1 FETVKLYKKGQVV---GTVKVWKGKEKTVKLGAKEDVYVTLPKG--EKKKLKAKVVL-DKPELEAPIKKGQVVGTL--VV 72
|
90 100
....*....|....*....|.
gi 2189018674 423 KDNGlEQKKTVNLIASEEVEK 443
Cdd:smart00936 73 TLDG-KLIGEVPLVALEDVEK 92
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
86-238 |
1.17e-10 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 62.22 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 86 TGQVlVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVT-TSEHASLTRGSRIFLAEGDKHTVRDLYIAMAIGSA 164
Cdd:COG2367 44 TGET-VGINADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTlTPEDLVGGSGILQKLPDGTGLTLRELAELMITVSD 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2189018674 165 NDATVALAERIaGTEKefanlMNETAKKLGMTTahfinsTGLGReDMPEKFRPEGTDETVMSAMDVAKLVRAIV 238
Cdd:COG2367 123 NTATNLLLRLL-GPDA-----VNAFLRSLGLTD------TRLDR-KEPDLNELPGDGRNTTTPRDMARLLAALY 183
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
343-443 |
1.16e-09 |
|
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: 54.91 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 343 YEVQPVVAPKQAVdgvAAAPIKKGVSTEVPVVPENGVNFVVPKGAstEGKITHEVKLTpaNELIAPIKNGQKIGTITFtY 422
Cdd:pfam07943 1 FETKKLYKKGDVV---KKVKVWKGKKKTVPLGAKEDVYVTVPKGE--KKKLKAKVTLK--KPLEAPIKKGQVVGKLEV-Y 72
|
90 100
....*....|....*....|.
gi 2189018674 423 KDNglEQKKTVNLIASEEVEK 443
Cdd:pfam07943 73 LDG--KLIGEVPLVAKEDVEE 91
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
85-238 |
1.28e-09 |
|
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.
Pssm-ID: 463854 [Multi-domain] Cd Length: 215 Bit Score: 58.05 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189018674 85 STGQVlVNIDSNTPKPPASMTKMMTEYIVMEKVKNGELSWEEEVTTSEhASLTRGSRIF--LAEGDKHTVRDLYIAMAIG 162
Cdd:pfam13354 8 DTGEE-LGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTA-EDKVGGSGILqyLPDGSQLSLRDLLTLMIAV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2189018674 163 SANDATVALAERIaGTEKefanlMNETAKKLGMTTAHFINstglgreDMPEKFRPEGTDETVMSAMDVAKLVRAIV 238
Cdd:pfam13354 86 SDNTATNLLIDRL-GLEA-----VNARLRALGLRDTRLRR-------KLPDLRAADKGGTNTTTARDMAKLLEALY 148
|
|
| |
