|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
43-403 |
1.25e-104 |
|
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: 315.66 E-value: 1.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNNEFSNVPFEKgRQYTVRELYHSIVI 122
Cdd:NF038273 38 TGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDYPYELTTNYEISNVPLDA-RKYTVKELLEASLV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKGKHPEGTDPNAENSMSARDMGILSKAMIT 202
Cdd:NF038273 117 ASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 203 KYPEMLEDTKQRFRNFPDNhpkpiRMENWNWMLPGAAFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:NF038273 197 DFPEVLKITSKTSADFAGT-----TIYSYNYMLKGMPYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNAD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 283 E----RFTESRELIEYGFNNFEKQKL----KVDKNNTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlae 354
Cdd:NF038273 272 EdeyaRFTATNQLLDYIYQNFEKVTLvkkgQAYKDSKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK--- 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446645492 355 dgHLVAPIKKDAKVGSITLESTDKYG--FLDGSKSMKVTAKttEEVEKANW 403
Cdd:NF038273 349 --ELTAPIKKGQVVGKATFKDKDLIGkgYLGEPPSVELVAK--KDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
43-404 |
1.32e-93 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 284.42 E-value: 1.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVsrnnEFSNVPFEKGRQYTVRELYHSIVI 122
Cdd:COG1686 38 TGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnadlkgkhpegtdPNAENSMSARDMGILSKAMIT 202
Cdd:COG1686 114 QSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGL--------------PDPGHYSTARDLALLARAAIK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 203 KYPEMLEDTKQRFRNFPDnhPKPIRMENWNWMLpgaaFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:COG1686 180 DYPEFYEIFSTKEFTFPN--GRGITLRNTNRLL----GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 283 ERFTESRELIEYGFnnfekqklkvdknntlsvvqgkedqvtvapekeitviakkgsknpyKIGTEVDKSLAEDGHLVAPI 362
Cdd:COG1686 254 ARFADAAKLLDYGF----------------------------------------------PKGEALKAEVVLDGPLKAPV 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446645492 363 KKDAKVGSITLestdkygFLDGSKSMKVTAKTTEEVEKANWF 404
Cdd:COG1686 288 KKGQVVGTLVV-------TLDGKTIAEVPLVAAEDVEKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
43-276 |
8.56e-64 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 204.93 E-value: 8.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSrNNEFSNVPFEKGRQYTVRELYHSIVI 122
Cdd:pfam00768 18 TGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATG-NPGSSNIFLKPGSQVSVKDLLRGALV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKgkhpegtdpnaensMSARDMGILSKAMIT 202
Cdd:pfam00768 97 SSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQY--------------SSARDMAILAKALIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446645492 203 KYPEMLEDTKQRFRNFPDnhpkpirMENWNWMLPGAAFAYEG--TDGLKTGSSDTAGYGFTITAKRGDVRLISVII 276
Cdd:pfam00768 163 DLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASATKGGMRLISVVM 231
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
43-423 |
4.93e-45 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 160.93 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNN-EFSNVPFEK-GRQYTVRELYHSI 120
Cdd:PRK10001 49 SGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPAlRGSSVMFLKpGDQVSVADLNKGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 121 VIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGILSKAM 200
Cdd:PRK10001 129 IIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL---DAPGQFS-----------TARDMALLGKAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 201 ITKYPEMLEDTKQRFRNFpdnhpKPIRMENWNWMLPGAAFayeGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKS 280
Cdd:PRK10001 195 IHDVPEEYAIHKEKEFTF-----NKIRQPNRNRLLWSSNL---NVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 281 MDERFTESRELIEYGFNNFEK-QKLKVDKN-NTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDkslaeDGHL 358
Cdd:PRK10001 267 DRIRFNESEKLLTWGFRFFETvTPIKPDATfVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLT-----EPQL 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446645492 359 VAPIKKDAKVGSITLESTDKygfldgsksmkvtaktteEVEKANWFVLTMRSIGDFFSNLWSKVF 423
Cdd:PRK10001 342 TAPLKKGQVVGTIDFQLNGK------------------SIEQRPLIVMENVEEGGFFSRMWDFVM 388
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
299-400 |
1.94e-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: 198004 [Multi-domain] Cd Length: 92 Bit Score: 54.14 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 299 FEKQKLkVDKN---NTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlaedgHLVAPIKKDAKVGSITLes 375
Cdd:smart00936 1 FETVKL-YKKGqvvGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKP-----ELEAPIKKGQVVGTLVV-- 72
|
90 100
....*....|....*....|....*
gi 446645492 376 tdkygFLDGSKSMKVTAKTTEEVEK 400
Cdd:smart00936 73 -----TLDGKLIGEVPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
43-403 |
1.25e-104 |
|
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: 315.66 E-value: 1.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNNEFSNVPFEKgRQYTVRELYHSIVI 122
Cdd:NF038273 38 TGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDYPYELTTNYEISNVPLDA-RKYTVKELLEASLV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKGKHPEGTDPNAENSMSARDMGILSKAMIT 202
Cdd:NF038273 117 ASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 203 KYPEMLEDTKQRFRNFPDNhpkpiRMENWNWMLPGAAFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:NF038273 197 DFPEVLKITSKTSADFAGT-----TIYSYNYMLKGMPYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNAD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 283 E----RFTESRELIEYGFNNFEKQKL----KVDKNNTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlae 354
Cdd:NF038273 272 EdeyaRFTATNQLLDYIYQNFEKVTLvkkgQAYKDSKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK--- 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446645492 355 dgHLVAPIKKDAKVGSITLESTDKYG--FLDGSKSMKVTAKttEEVEKANW 403
Cdd:NF038273 349 --ELTAPIKKGQVVGKATFKDKDLIGkgYLGEPPSVELVAK--KDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
43-404 |
1.32e-93 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 284.42 E-value: 1.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVsrnnEFSNVPFEKGRQYTVRELYHSIVI 122
Cdd:COG1686 38 TGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnadlkgkhpegtdPNAENSMSARDMGILSKAMIT 202
Cdd:COG1686 114 QSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGL--------------PDPGHYSTARDLALLARAAIK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 203 KYPEMLEDTKQRFRNFPDnhPKPIRMENWNWMLpgaaFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:COG1686 180 DYPEFYEIFSTKEFTFPN--GRGITLRNTNRLL----GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 283 ERFTESRELIEYGFnnfekqklkvdknntlsvvqgkedqvtvapekeitviakkgsknpyKIGTEVDKSLAEDGHLVAPI 362
Cdd:COG1686 254 ARFADAAKLLDYGF----------------------------------------------PKGEALKAEVVLDGPLKAPV 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446645492 363 KKDAKVGSITLestdkygFLDGSKSMKVTAKTTEEVEKANWF 404
Cdd:COG1686 288 KKGQVVGTLVV-------TLDGKTIAEVPLVAAEDVEKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
43-276 |
8.56e-64 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 204.93 E-value: 8.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSrNNEFSNVPFEKGRQYTVRELYHSIVI 122
Cdd:pfam00768 18 TGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATG-NPGSSNIFLKPGSQVSVKDLLRGALV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKgkhpegtdpnaensMSARDMGILSKAMIT 202
Cdd:pfam00768 97 SSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQY--------------SSARDMAILAKALIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446645492 203 KYPEMLEDTKQRFRNFPDnhpkpirMENWNWMLPGAAFAYEG--TDGLKTGSSDTAGYGFTITAKRGDVRLISVII 276
Cdd:pfam00768 163 DLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASATKGGMRLISVVM 231
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
43-423 |
4.93e-45 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 160.93 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNN-EFSNVPFEK-GRQYTVRELYHSI 120
Cdd:PRK10001 49 SGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPAlRGSSVMFLKpGDQVSVADLNKGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 121 VIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGILSKAM 200
Cdd:PRK10001 129 IIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL---DAPGQFS-----------TARDMALLGKAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 201 ITKYPEMLEDTKQRFRNFpdnhpKPIRMENWNWMLPGAAFayeGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKS 280
Cdd:PRK10001 195 IHDVPEEYAIHKEKEFTF-----NKIRQPNRNRLLWSSNL---NVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 281 MDERFTESRELIEYGFNNFEK-QKLKVDKN-NTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDkslaeDGHL 358
Cdd:PRK10001 267 DRIRFNESEKLLTWGFRFFETvTPIKPDATfVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLT-----EPQL 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446645492 359 VAPIKKDAKVGSITLESTDKygfldgsksmkvtaktteEVEKANWFVLTMRSIGDFFSNLWSKVF 423
Cdd:PRK10001 342 TAPLKKGQVVGTIDFQLNGK------------------SIEQRPLIVMENVEEGGFFSRMWDFVM 388
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
43-404 |
1.74e-36 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 137.68 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYeVSRNNEF--SNVPFEK-GRQYTVRELYHS 119
Cdd:PRK10793 56 SGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAW-ATGNPVFkgSSLMFLKpGMQVPVSQLIRG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 120 IVIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGILSKA 199
Cdd:PRK10793 135 INLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGL---DADGQYS-----------SARDMALIGQA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 200 MITKYPEmlEDTKQRFRNFPDNHpkpIRMENWNWMLPGAAFAyegTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTK 279
Cdd:PRK10793 201 LIRDVPN--EYAIYKEKEFTFNG---IRQLNRNGLLWDNSLN---VDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 280 SMDERFTESRELIEYGFNNFEK-QKLKVDKN-NTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlaedgH 357
Cdd:PRK10793 273 TFKGRETESKKLLTWGFRFFETvNPLKVGKEfASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTS-----E 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446645492 358 LVAPIKKDAKVGSITLEstdkygfLDGSKSMKVTAKTTEEVEKANWF 404
Cdd:PRK10793 348 LHAPLQKNQVVGTINFQ-------LDGKTIEQRPLVVLQEIPEGNFF 387
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
43-378 |
5.27e-35 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 133.41 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYeVSRNNEF--SNVPFEK-GRQYTVRELYHS 119
Cdd:PRK11397 46 TGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAW-AKDNPVFvgSSLMFLKeGDRVSVRDLSRG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 120 IVIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGILSKA 199
Cdd:PRK11397 125 LIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGL---DAPGQHS-----------SAYDLAVLSRA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 200 MITKYPEMLEDTKQRFRNFpdnhpKPIRMENWNWMLpgaafaYEGT---DGLKTGSSDTAGYGFTITAKRGDVRLISVII 276
Cdd:PRK11397 191 IIHGEPEFYHMYSEKSLTW-----NGITQQNRNGLL------WDKTmnvDGLKTGHTSGAGFNLIASAVDGQRRLIAVVM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 277 KTKSMDERFTESRELIEYGFNNFEKQKL--KVDKNNTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlae 354
Cdd:PRK11397 260 GADSAKGREEQARKLLRWGQQNFTTVQIlhRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGK--- 336
|
330 340
....*....|....*....|....
gi 446645492 355 dgHLVAPIKKDAKVGSITLESTDK 378
Cdd:PRK11397 337 --ELEAPISAHQRVGEIELYDRDK 358
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
299-400 |
6.42e-11 |
|
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: 58.37 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 299 FEKQKL--KVDKNNTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlaedghLVAPIKKDAKVGSITLest 376
Cdd:pfam07943 1 FETKKLykKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP------LEAPIKKGQVVGKLEV--- 71
|
90 100
....*....|....*....|....
gi 446645492 377 dkygFLDGSKSMKVTAKTTEEVEK 400
Cdd:pfam07943 72 ----YLDGKLIGEVPLVAKEDVEE 91
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
43-258 |
1.52e-10 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 62.01 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAikegKITWDTK--VNISDyAYEVsrNNEFSNVPFekGRQYTVRELYHSI 120
Cdd:PRK11669 51 TNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPLDEKlkVDISQ-TPEM--KGVYSRVRL--NSEISRKDMLLLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 121 VIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnadlkgkhpegtdpNAENSMSARDMGILSKAM 200
Cdd:PRK11669 122 LMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPTGL---------------SIHNVSTARDLTKLLIAS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446645492 201 iTKYPEM--LEDTKQR------------FRNfpDNHpkPIRMENWNWMLPgaafayegtdglKTGSSDTAGY 258
Cdd:PRK11669 187 -KQYPLIgqLSTTREKtatfrkpnytlpFRN--TNH--LVYRDNWNIQLT------------KTGFTNAAGH 241
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
43-292 |
1.85e-09 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 58.37 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 43 TGKILhEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEvsrnnEFSNV--PFEKGRQYTVRELYHSI 120
Cdd:COG2367 44 TGETV-GINADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLV-----GGSGIlqKLPDGTGLTLRELAELM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 121 VIFSANGSSIALAELLaGSEKnflnlANEHAKKLGLKKYKFVNATGLNNADLKGKhpegtdpnaENSMSARDMGILSKAM 200
Cdd:COG2367 118 ITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTRLDRKEPDLNELPGDG---------RNTTTPRDMARLLAAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 201 ITkyPEML-EDTKQRFRNFpdnhpkpirMEN--WNWMLP-----GAAFAYegtdglKTGSSDT----AGYgftITAKRGD 268
Cdd:COG2367 183 YR--GELLsPESRARLLDW---------LARqtGRDRLRaglpeGWRVAH------KTGTGGGvrndVGI---VWPPDGK 242
|
250 260
....*....|....*....|....
gi 446645492 269 VRLISVIIKTKSMDERftESRELI 292
Cdd:COG2367 243 PYVLAVFTKGPDADAA--RAEALI 264
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
299-400 |
1.94e-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: 198004 [Multi-domain] Cd Length: 92 Bit Score: 54.14 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 299 FEKQKLkVDKN---NTLSVVQGKEDQVTVAPEKEITVIAKKGSKNPYKIGTEVDKSlaedgHLVAPIKKDAKVGSITLes 375
Cdd:smart00936 1 FETVKL-YKKGqvvGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKP-----ELEAPIKKGQVVGTLVV-- 72
|
90 100
....*....|....*....|....*
gi 446645492 376 tdkygFLDGSKSMKVTAKTTEEVEK 400
Cdd:smart00936 73 -----TLDGKLIGEVPLVALEDVEK 92
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
51-194 |
3.50e-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: 50.74 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 51 NPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDyayEVSRNNEFSNVPFEKGRQYTVRELYHSIVIFSANGSSI 130
Cdd:pfam13354 16 NGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTA---EDKVGGSGILQYLPDGSQLSLRDLLTLMIAVSDNTATN 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446645492 131 ALAELLAGSEknflnlANEHAKKLGLKkykfvnATGLNNADLKgkhPEGTDPNAENSMSARDMG 194
Cdd:pfam13354 93 LLIDRLGLEA------VNARLRALGLR------DTRLRRKLPD---LRAADKGGTNTTTARDMA 141
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
44-90 |
2.81e-04 |
|
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
Pssm-ID: 441286 [Multi-domain] Cd Length: 355 Bit Score: 42.75 E-value: 2.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645492 44 GKILHEQ-------------NPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVniSDY 90
Cdd:COG1680 43 GKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDDPV--SKY 100
|
|
| Beta-lactamase |
pfam00144 |
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ... |
51-116 |
1.97e-03 |
|
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.
Pssm-ID: 395092 [Multi-domain] Cd Length: 327 Bit Score: 40.18 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446645492 51 NPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVniSDYayevsrnnefsnVPFEKGRQY---TVREL 116
Cdd:pfam00144 45 TADTLFRIASVTKTFTAAAVLQLVERGKLDLDDPV--SKY------------LPEFAGPGKggiTLRDL 99
|
|
| |
