|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
4-408 |
1.76e-121 |
|
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: 359.18 E-value: 1.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 4 KRFIALVtMLTLACSMLLPysnASAEtgaALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGK 83
Cdd:NF038273 1 KKLILLL-LLLLAFFLATT---VSAD---DFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 84 LKWDQKIKVSEYAYKVSQDASLSNVALENGgSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKN 163
Cdd:NF038273 74 LSWDTPVKISDYPYELTTNYEISNVPLDAR-KYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 164 YKFVNSTGLTNKDLKGMHPEGTTADEENKMSAKDVATLAQHLIKDYPKVLDTAKIPKKEFRPEKekfaMSNWNWMLKGLV 243
Cdd:NF038273 153 AKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFAGTT----IYSYNYMLKGMP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 244 KEYDGVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKT----SSHTARFDETKKLYDYGFANFEMKQMYKKGSSVKgQE 319
Cdd:NF038273 229 YYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNAdnadEDEYARFTATNQLLDYIYQNFEKVTLVKKGQAYK-DS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 320 TVRVENAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQmvITPKDTND--PGFLtGKSLQVDL 397
Cdd:NF038273 308 KLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKKELTAPIKKGQVVGK--ATFKDKDLigKGYL-GEPPSVEL 384
|
410
....*....|.
gi 501805092 398 VTTAEVEEANW 408
Cdd:NF038273 385 VAKKDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
4-411 |
2.41e-112 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 332.96 E-value: 2.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 4 KRFIALVTMLTLAcsmllpysNASAETGAALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGK 83
Cdd:COG1686 2 KKLLLLALLLLLA--------AAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 84 LKWDQKIKVSEYAYKVsqdaSLSNVALENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKN 163
Cdd:COG1686 74 ISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 164 YKFVNSTGLTnkdlkgmhpegttaDEENKMSAKDVATLAQHLIKDYPKVLDTAKIPKKEFrPEKEKFAMSNWNWMLkglv 243
Cdd:COG1686 150 THFVNPTGLP--------------DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTF-PNGRGITLRNTNRLL---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 244 KEYDGVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKTSSHTARFDETKKLYDYGFanfemkqmykkgssvkgqetvrv 323
Cdd:COG1686 211 GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF----------------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 324 enakdkdvavqtkqaislpvPKGSKDVYKTELKESSKgqeAPIKKGAALGQMVITpkdtndpgfLTGKSL-QVDLVTTAE 402
Cdd:COG1686 268 --------------------PKGEALKAEVVLDGPLK---APVKKGQVVGTLVVT---------LDGKTIaEVPLVAAED 315
|
....*....
gi 501805092 403 VEEANWFTR 411
Cdd:COG1686 316 VEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
32-280 |
8.98e-83 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 254.23 E-value: 8.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 32 AALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGKLKWDQKIKVSEYAYKVSQDASlSNVALE 111
Cdd:pfam00768 2 SAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 112 NGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKNYKFVNSTGLTNkdlkgmhpegttadEEN 191
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDA--------------HGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 192 KMSAKDVATLAQHLIKDYPKVLDTAKIPKKEFRpekekfAMSNWNWMLKGLVKEYDG--VDGLKTGSTPEAGDCFTGTVE 269
Cdd:pfam00768 147 YSSARDMAILAKALIKDLPEELSITKEKSFTFR------GINKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASAT 220
|
250
....*....|.
gi 501805092 270 RNGMRFISVVI 280
Cdd:pfam00768 221 KGGMRLISVVM 231
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
13-435 |
2.69e-48 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 169.79 E-value: 2.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 13 LTLACSMLL---PYSNASAETGAALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGKLKWDQK 89
Cdd:PRK10001 11 LAAGSAFLFlfaPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 90 IKVSEYAYKVSQDA--SLSNVALENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKNYKFV 167
Cdd:PRK10001 91 VTVGKDAWATGNPAlrGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 168 NSTGLtnkDLKGMHPegttadeenkmSAKDVATLAQHLIKDYPKVLDTAKipKKEFRPEKEKFAMSN---WNWMLKglvk 244
Cdd:PRK10001 171 TVHGL---DAPGQFS-----------TARDMALLGKALIHDVPEEYAIHK--EKEFTFNKIRQPNRNrllWSSNLN---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 245 eydgVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKTSSHTARFDETKKLYDYGFANFEMKQMYKKGSSVKGQetvRVE 324
Cdd:PRK10001 231 ----VDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQ---RVW 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 325 NAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQMVITpkdtndpgfLTGKSL-QVDLVTTAEV 403
Cdd:PRK10001 304 FGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQ---------LNGKSIeQRPLIVMENV 374
|
410 420 430
....*....|....*....|....*....|..
gi 501805092 404 EEanwftramrgiGSFFSGIWNSAVDTVKGWF 435
Cdd:PRK10001 375 EE-----------GGFFSRMWDFVMMKFHQWF 395
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
303-405 |
2.92e-17 |
|
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: 76.49 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 303 FEMKQMYKKGSSVKgqeTVRVENAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQMVITpkdt 382
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVT---- 73
|
90 100
....*....|....*....|...
gi 501805092 383 nDPGFLTGKslqVDLVTTAEVEE 405
Cdd:smart00936 74 -LDGKLIGE---VPLVALEDVEK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
4-408 |
1.76e-121 |
|
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: 359.18 E-value: 1.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 4 KRFIALVtMLTLACSMLLPysnASAEtgaALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGK 83
Cdd:NF038273 1 KKLILLL-LLLLAFFLATT---VSAD---DFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 84 LKWDQKIKVSEYAYKVSQDASLSNVALENGgSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKN 163
Cdd:NF038273 74 LSWDTPVKISDYPYELTTNYEISNVPLDAR-KYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 164 YKFVNSTGLTNKDLKGMHPEGTTADEENKMSAKDVATLAQHLIKDYPKVLDTAKIPKKEFRPEKekfaMSNWNWMLKGLV 243
Cdd:NF038273 153 AKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFAGTT----IYSYNYMLKGMP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 244 KEYDGVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKT----SSHTARFDETKKLYDYGFANFEMKQMYKKGSSVKgQE 319
Cdd:NF038273 229 YYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNAdnadEDEYARFTATNQLLDYIYQNFEKVTLVKKGQAYK-DS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 320 TVRVENAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQmvITPKDTND--PGFLtGKSLQVDL 397
Cdd:NF038273 308 KLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKKELTAPIKKGQVVGK--ATFKDKDLigKGYL-GEPPSVEL 384
|
410
....*....|.
gi 501805092 398 VTTAEVEEANW 408
Cdd:NF038273 385 VAKKDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
4-411 |
2.41e-112 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 332.96 E-value: 2.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 4 KRFIALVTMLTLAcsmllpysNASAETGAALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGK 83
Cdd:COG1686 2 KKLLLLALLLLLA--------AAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 84 LKWDQKIKVSEYAYKVsqdaSLSNVALENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKN 163
Cdd:COG1686 74 ISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 164 YKFVNSTGLTnkdlkgmhpegttaDEENKMSAKDVATLAQHLIKDYPKVLDTAKIPKKEFrPEKEKFAMSNWNWMLkglv 243
Cdd:COG1686 150 THFVNPTGLP--------------DPGHYSTARDLALLARAAIKDYPEFYEIFSTKEFTF-PNGRGITLRNTNRLL---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 244 KEYDGVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKTSSHTARFDETKKLYDYGFanfemkqmykkgssvkgqetvrv 323
Cdd:COG1686 211 GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEKARFADAAKLLDYGF----------------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 324 enakdkdvavqtkqaislpvPKGSKDVYKTELKESSKgqeAPIKKGAALGQMVITpkdtndpgfLTGKSL-QVDLVTTAE 402
Cdd:COG1686 268 --------------------PKGEALKAEVVLDGPLK---APVKKGQVVGTLVVT---------LDGKTIaEVPLVAAED 315
|
....*....
gi 501805092 403 VEEANWFTR 411
Cdd:COG1686 316 VEKAGFFSR 324
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
32-280 |
8.98e-83 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 254.23 E-value: 8.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 32 AALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGKLKWDQKIKVSEYAYKVSQDASlSNVALE 111
Cdd:pfam00768 2 SAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 112 NGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKNYKFVNSTGLTNkdlkgmhpegttadEEN 191
Cdd:pfam00768 81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDA--------------HGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 192 KMSAKDVATLAQHLIKDYPKVLDTAKIPKKEFRpekekfAMSNWNWMLKGLVKEYDG--VDGLKTGSTPEAGDCFTGTVE 269
Cdd:pfam00768 147 YSSARDMAILAKALIKDLPEELSITKEKSFTFR------GINKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASAT 220
|
250
....*....|.
gi 501805092 270 RNGMRFISVVI 280
Cdd:pfam00768 221 KGGMRLISVVM 231
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
13-435 |
2.69e-48 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 169.79 E-value: 2.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 13 LTLACSMLL---PYSNASAETGAALNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGKLKWDQK 89
Cdd:PRK10001 11 LAAGSAFLFlfaPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 90 IKVSEYAYKVSQDA--SLSNVALENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKNYKFV 167
Cdd:PRK10001 91 VTVGKDAWATGNPAlrGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 168 NSTGLtnkDLKGMHPegttadeenkmSAKDVATLAQHLIKDYPKVLDTAKipKKEFRPEKEKFAMSN---WNWMLKglvk 244
Cdd:PRK10001 171 TVHGL---DAPGQFS-----------TARDMALLGKALIHDVPEEYAIHK--EKEFTFNKIRQPNRNrllWSSNLN---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 245 eydgVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKTSSHTARFDETKKLYDYGFANFEMKQMYKKGSSVKGQetvRVE 324
Cdd:PRK10001 231 ----VDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQ---RVW 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 325 NAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQMVITpkdtndpgfLTGKSL-QVDLVTTAEV 403
Cdd:PRK10001 304 FGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQ---------LNGKSIeQRPLIVMENV 374
|
410 420 430
....*....|....*....|....*....|..
gi 501805092 404 EEanwftramrgiGSFFSGIWNSAVDTVKGWF 435
Cdd:PRK10001 375 EE-----------GGFFSRMWDFVMMKFHQWF 395
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
15-411 |
1.04e-38 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 143.81 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 15 LACSMLLPYSNASAETGAALN-------IEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAVDKGKLKWD 87
Cdd:PRK11397 6 IIAASLFAFNLSSAFAAENIPfspqppaIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 88 QKIKVSEYAYK----VSQDASLsnVALENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDKSKELGLKN 163
Cdd:PRK11397 86 DIVTVGRDAWAkdnpVFVGSSL--MFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 164 YKFVNSTGLtnkDLKGMHPegttadeenkmSAKDVATLAQHLIKDYPkvldtakipkKEFRPEKEKfaMSNWNWMLK--- 240
Cdd:PRK11397 164 THFETVHGL---DAPGQHS-----------SAYDLAVLSRAIIHGEP----------EFYHMYSEK--SLTWNGITQqnr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 241 -GLVkeYD---GVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKTSSHTARFDETKKLYDYGFANFEMKQMYKKGSSVk 316
Cdd:PRK11397 218 nGLL--WDktmNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKV- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 317 GQEtvRVENAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQMVITPKDtndpgfltgKSL-QV 395
Cdd:PRK11397 295 GTE--RIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGKELEAPISAHQRVGEIELYDRD---------KQVaHW 363
|
410
....*....|....*.
gi 501805092 396 DLVTTAEVEEANWFTR 411
Cdd:PRK11397 364 PLVTLESVGEGGMFSR 379
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
5-420 |
1.85e-37 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 140.76 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 5 RFIALVTMLTLACSMLLPYSNASAETGAAL-----NIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHEAV 79
Cdd:PRK10793 8 RIMKRLALTTALCTAFISAAHADDLNIKTMipgvpQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 80 DKGKLKWDQKIKVSEYAYK----VSQDASLsnVALENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMNDK 155
Cdd:PRK10793 88 KAGKFKETDLVTVGNDAWAtgnpVFKGSSL--MFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 156 SKELGLKNYKFvnstgltnKDLKGMHPEGTTAdeenkmSAKDVATLAQHLIKDYPkvldtakipkKEFRPEKEK-FAMSN 234
Cdd:PRK10793 166 VNALGLKNTHF--------QTVHGLDADGQYS------SARDMALIGQALIRDVP----------NEYAIYKEKeFTFNG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 235 WNWMLK-GLVKEYD-GVDGLKTGSTPEAGDCFTGTVERNGMRFISVVIKTSSHTARFDETKKLYDYGFANFEMKQMYKKG 312
Cdd:PRK10793 222 IRQLNRnGLLWDNSlNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 313 SSVKGQ-----ETVRVENAKDKDVavqtkqaiSLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQMVITpkdtndpgf 387
Cdd:PRK10793 302 KEFASEpvwfgDSDRASLGVDKDV--------YLTIPRGRMKDLKASYVLNTSELHAPLQKNQVVGTINFQ--------- 364
|
410 420 430
....*....|....*....|....*....|....
gi 501805092 388 LTGKSL-QVDLVTTAEVEEANWFTRAMRGIGSFF 420
Cdd:PRK10793 365 LDGKTIeQRPLVVLQEIPEGNFFGKIIDYIKLMF 398
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
4-263 |
1.15e-18 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 86.27 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 4 KRFIALVTMLTLACSMLLPYSNASAETGAA------LNIEAGAAILVEANSGKIVYQKNADELLSIASMTKMMSEYLVHE 77
Cdd:PRK11669 1 MKFRVSLLSLLLLLAGVPFAPQAVAKTAAAttasqpQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 78 AvdkgKLKWDQKIKVseyayKVSQDASL----SNVALenGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVDFVKMMN 153
Cdd:PRK11669 81 A----KLPLDEKLKV-----DISQTPEMkgvySRVRL--NSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 154 DKSKELGLKNYKFVNSTGLTnkdlkgmhpegttadEENKMSAKDVATLaqhLI--KDYPKVLDTAKIPKK---------- 221
Cdd:PRK11669 150 AKAKALGMTNTRYVEPTGLS---------------IHNVSTARDLTKL---LIasKQYPLIGQLSTTREKtatfrkpnyt 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 501805092 222 -EFRPEKEKFAMSNWNWMLKglvkeydgvdglKTGSTPEAGDC 263
Cdd:PRK11669 212 lPFRNTNHLVYRDNWNIQLT------------KTGFTNAAGHC 242
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
303-405 |
2.92e-17 |
|
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: 76.49 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 303 FEMKQMYKKGSSVKgqeTVRVENAKDKDVAVQTKQAISLPVPKGSKDVYKTELKESSKGQEAPIKKGAALGQMVITpkdt 382
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKPELEAPIKKGQVVGTLVVT---- 73
|
90 100
....*....|....*....|...
gi 501805092 383 nDPGFLTGKslqVDLVTTAEVEE 405
Cdd:smart00936 74 -LDGKLIGE---VPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
303-405 |
5.98e-15 |
|
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: 69.93 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 303 FEMKQMYKKGSSVKgqeTVRVENAKDKDVAVQTKQAISLPVPKGSKDVYKTELkESSKGQEAPIKKGAALGQMVItpkdt 382
Cdd:pfam07943 1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKV-TLKKPLEAPIKKGQVVGKLEV----- 71
|
90 100
....*....|....*....|....
gi 501805092 383 ndpgFLTGKSL-QVDLVTTAEVEE 405
Cdd:pfam07943 72 ----YLDGKLIgEVPLVAKEDVEE 91
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
4-205 |
2.27e-10 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 61.07 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 4 KRFIALVTMLTLACSMLLPYSNASAETGAALNIEAGAAILvEANSGKIVYQkNADELLSIASMTKMMSEYLVHEAVDKGK 83
Cdd:COG2367 1 MRLLALLLLAAAAAAPASALEAELAALEAALGGRVGVYVL-DLDTGETVGI-NADERFPAASTFKLPVLAAVLRQVDAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 84 LKWDQKIKVSEyAYKVSQDASLSNvaLENGGSYTVKELYEAMAIFSANGATIALAEAIAGKEVdfvkmmNDKSKELGLKN 163
Cdd:COG2367 79 LSLDERVTLTP-EDLVGGSGILQK--LPDGTGLTLRELAELMITVSDNTATNLLLRLLGPDAV------NAFLRSLGLTD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501805092 164 ykfvnstglTNKDLKGMHPEGTTADEENKMSAKDVATLAQHL 205
Cdd:COG2367 150 ---------TRLDRKEPDLNELPGDGRNTTTPRDMARLLAAL 182
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
52-208 |
1.11e-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: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 52 VYQKNADELLSIASMTKMMSEYLVHEAVDKGKLKWDQKIKVSEyAYKVSQDASLSNvaLENGGSYTVKELYEAMAIFSAN 131
Cdd:pfam13354 12 ELGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTA-EDKVGGSGILQY--LPDGSQLSLRDLLTLMIAVSDN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501805092 132 GATIALAEAIAGKEVdfvkmmNDKSKELGLKNykfvnstglTNKDLKGMHPEGTTADEENKMSAKDVATLAQHLIKD 208
Cdd:pfam13354 89 TATNLLIDRLGLEAV------NARLRALGLRD---------TRLRRKLPDLRAADKGGTNTTTARDMAKLLEALYRG 150
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
39-95 |
1.29e-05 |
|
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
Pssm-ID: 441286 [Multi-domain] Cd Length: 355 Bit Score: 46.99 E-value: 1.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 39 GAAILVeANSGKIVYQK-------------NADELLSIASMTKMMSEYLVHEAVDKGKLKWDQkiKVSEY 95
Cdd:COG1680 34 GAAVAV-VRDGKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDD--PVSKY 100
|
|
| Beta-lactamase |
pfam00144 |
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ... |
39-95 |
1.09e-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: 40.95 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501805092 39 GAAILVeANSGKIVYQK-------------NADELLSIASMTKMMSEYLVHEAVDKGKLKWDQkiKVSEY 95
Cdd:pfam00144 16 GVAVAV-TRDGKVVVDRgggvadleggrpvTADTLFRIASVTKTFTAAAVLQLVERGKLDLDD--PVSKY 82
|
|
| |
