|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
27-363 |
1.05e-40 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 151.00 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 27 ASVQEIIN----AAVPVANDYGLYPSVMIAQGILESSGGQSALASNYN-NIFGVKYTSGTPIYlpTQEYL----NGTMTN 97
Cdd:PRK06347 148 ATVQSFIQtiqaSSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSY--TKQTLeddgKGNYYT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 98 VVEPFQAYSSVYDACVAQAKMLRA-----SSYYSGAWRENTSSYLDATAWLEGRYATDPTYASKLNSVISELGLSVYDQG 172
Cdd:PRK06347 226 ITAKFRKYPSYHQSLEDYAQVIRKgpswnPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSG 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 173 GEISG-----GTAVTTSSSASTNSAGTYKVQEGDSLSAIAAQYGTTVDALVSANSLENANdIHVGEVLQVAGASTTTTTT 247
Cdd:PRK06347 306 KTTGGnsgstGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDF-IYPGQKLKVSAGSTTSDTN 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 248 ST----------NTTSNVSSSSTYTVKSGDSLYSIAEQYGMTVSSLMSANGIYdvNSMLQVGQVLQVTVSTSA------- 310
Cdd:PRK06347 385 TSkpstgtstskPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLK--SDFIYPGQKLKVSAGSTSntntskp 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046562299 311 ---------TTSNTTTSNSYTIQNGDSIYSIATANGMTADQLAALNGFGiNDMIHPGQTIRI 363
Cdd:PRK06347 463 stntntskpSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLK-SDFIYPGQKLKV 523
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
2-167 |
6.20e-39 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 139.72 E-value: 6.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 2 KQKHKLALGASIVALASLGGIKAQAASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSAL-ASNYNNIFGVKYTSG 80
Cdd:COG1705 106 ALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 81 TP---IYLPTQEYLNGTMTNVVEPFQAYSSVYDACVAQAKMLRASSYYSGAWReNTSSYLDATAWL-EGRYATDPTYASK 156
Cdd:COG1705 186 WQgksVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALA-NAKDYEAFAKALqKAGYATDPKYADK 264
|
170
....*....|.
gi 1046562299 157 LNSVISELGLS 167
Cdd:COG1705 265 LISIIESYNLT 275
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
23-162 |
5.56e-24 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 95.97 E-value: 5.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 23 KAQAASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSALASNYNNIFGVKYTS-GTPIYLPTQEYLNGTMTNVVEP 101
Cdd:smart00047 6 GSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYdGRPVRMGTLEYLNGGWVTVKAA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046562299 102 FQAYSSVYDAcvAQAKMLRAS-SYYSGAWrentssylDATAWLEGRYATDPTYASKLNSVIS 162
Cdd:smart00047 86 FRGYFGEKFI--DYAYVLRGQnPLYKKRW--------GSNALQTAGYATDPDYAKKLIRIIA 137
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
34-115 |
2.44e-16 |
|
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.
Pssm-ID: 460354 [Multi-domain] Cd Length: 91 Bit Score: 73.38 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 34 NAAVPVANDYGLYPSVMIAQGILESSGGQSALASNYNNIFGVKYTSGTPIYLPTQEYlngtmtNVVEPFQAYSSVYDACV 113
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGKVAYDTDEV------TVAARFRKYDSVEESIR 75
|
..
gi 1046562299 114 AQ 115
Cdd:pfam01832 76 DY 77
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
24-164 |
1.41e-15 |
|
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.
Pssm-ID: 274188 [Multi-domain] Cd Length: 294 Bit Score: 76.04 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 24 AQAASVQEIINAAVPVAND----YGLYPSVMIAQGILESSGGQSAL----ASNYNNIFGVKYTS---GTPIYLPTQEYLN 92
Cdd:TIGR02541 143 SVPGHPKSFVNSMLPHARKaaqqLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKASGswqGKVVTTMTTEYVD 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046562299 93 GTMTNVVEPFQAYSSVYDACVAQAKMLRASSYYSGAWRENtSSYLDATAWLEGRYATDPTYASKLNSVISEL 164
Cdd:TIGR02541 223 GVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYEAVLQQR-SAESFARGLQRAGYATDPRYARKLLQVIQSL 293
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
30-170 |
9.82e-14 |
|
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
Pssm-ID: 411609 [Multi-domain] Cd Length: 312 Bit Score: 70.93 E-value: 9.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 30 QEIINAAVPVAN----DYGLYPSVMIAQGILESSGGQSALASNYNNIFGVK-------YTSGTPIYLPTQEYLNGTMTNV 98
Cdd:NF038016 161 AQFIAAVAPPAQqsqrATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfgspgpIAVGCRSYATFECSPTGGCFDT 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046562299 99 VEPFQAYSSVYDACVAQAKMLRASSYYSGA--WRENTSSYLDATaWLEGrYATDPTYASKLNSVISELGLSVYD 170
Cdd:NF038016 241 TATFRAYASAADSFRDHGRFLSVNSRYAPAfaYTDDPDQFAREI-HKAG-YATDPTYADKLIGLMKQYNLYQYD 312
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
194-237 |
1.24e-12 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 61.73 E-value: 1.24e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1046562299 194 TYKVQEGDSLSAIAAQYGTTVDALVSANSLENANDIHVGEVLQV 237
Cdd:cd00118 2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
27-363 |
1.05e-40 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 151.00 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 27 ASVQEIIN----AAVPVANDYGLYPSVMIAQGILESSGGQSALASNYN-NIFGVKYTSGTPIYlpTQEYL----NGTMTN 97
Cdd:PRK06347 148 ATVQSFIQtiqaSSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSY--TKQTLeddgKGNYYT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 98 VVEPFQAYSSVYDACVAQAKMLRA-----SSYYSGAWRENTSSYLDATAWLEGRYATDPTYASKLNSVISELGLSVYDQG 172
Cdd:PRK06347 226 ITAKFRKYPSYHQSLEDYAQVIRKgpswnPNYYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSG 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 173 GEISG-----GTAVTTSSSASTNSAGTYKVQEGDSLSAIAAQYGTTVDALVSANSLENANdIHVGEVLQVAGASTTTTTT 247
Cdd:PRK06347 306 KTTGGnsgstGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDF-IYPGQKLKVSAGSTTSDTN 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 248 ST----------NTTSNVSSSSTYTVKSGDSLYSIAEQYGMTVSSLMSANGIYdvNSMLQVGQVLQVTVSTSA------- 310
Cdd:PRK06347 385 TSkpstgtstskPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLK--SDFIYPGQKLKVSAGSTSntntskp 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046562299 311 ---------TTSNTTTSNSYTIQNGDSIYSIATANGMTADQLAALNGFGiNDMIHPGQTIRI 363
Cdd:PRK06347 463 stntntskpSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLK-SDFIYPGQKLKV 523
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
2-167 |
6.20e-39 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 139.72 E-value: 6.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 2 KQKHKLALGASIVALASLGGIKAQAASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSAL-ASNYNNIFGVKYTSG 80
Cdd:COG1705 106 ALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 81 TP---IYLPTQEYLNGTMTNVVEPFQAYSSVYDACVAQAKMLRASSYYSGAWReNTSSYLDATAWL-EGRYATDPTYASK 156
Cdd:COG1705 186 WQgksVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGALA-NAKDYEAFAKALqKAGYATDPKYADK 264
|
170
....*....|.
gi 1046562299 157 LNSVISELGLS 167
Cdd:COG1705 265 LISIIESYNLT 275
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
22-170 |
7.17e-26 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 108.72 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 22 IKAQAASVQEIinaavpvANDYGLYPSVMIAQGILESSGGQSALA-SNYNNIFGVK--YtSGTPIYLPTQEYLNGTMTNV 98
Cdd:PRK08581 324 IKSIAKDAHRI-------GQDNDIYASVMIAQAILESDSGQSALAkSPNHNLFGIKgaY-EGNSVSFNTLEADGNQLYSI 395
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046562299 99 VEPFQAYSSVYDACVAQAKMLRA-----SSYYSGAWRENTSSYLDATAWLEGRYATDPTYASKLNSVISELGLSVYD 170
Cdd:PRK08581 396 NAGFRKYPSTKESLEDYADLIKNgidgnSTIYKPTWKSEAKSYKDATSHLSKTYATDPNYAKKLNSIIKHYNLTQFD 472
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
23-162 |
5.56e-24 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 95.97 E-value: 5.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 23 KAQAASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSALASNYNNIFGVKYTS-GTPIYLPTQEYLNGTMTNVVEP 101
Cdd:smart00047 6 GSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYdGRPVRMGTLEYLNGGWVTVKAA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046562299 102 FQAYSSVYDAcvAQAKMLRAS-SYYSGAWrentssylDATAWLEGRYATDPTYASKLNSVIS 162
Cdd:smart00047 86 FRGYFGEKFI--DYAYVLRGQnPLYKKRW--------GSNALQTAGYATDPDYAKKLIRIIA 137
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
34-115 |
2.44e-16 |
|
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.
Pssm-ID: 460354 [Multi-domain] Cd Length: 91 Bit Score: 73.38 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 34 NAAVPVANDYGLYPSVMIAQGILESSGGQSALASNYNNIFGVKYTSGTPIYLPTQEYlngtmtNVVEPFQAYSSVYDACV 113
Cdd:pfam01832 2 PAAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKGKVAYDTDEV------TVAARFRKYDSVEESIR 75
|
..
gi 1046562299 114 AQ 115
Cdd:pfam01832 76 DY 77
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
24-164 |
1.41e-15 |
|
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.
Pssm-ID: 274188 [Multi-domain] Cd Length: 294 Bit Score: 76.04 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 24 AQAASVQEIINAAVPVAND----YGLYPSVMIAQGILESSGGQSAL----ASNYNNIFGVKYTS---GTPIYLPTQEYLN 92
Cdd:TIGR02541 143 SVPGHPKSFVNSMLPHARKaaqqLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKASGswqGKVVTTMTTEYVD 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046562299 93 GTMTNVVEPFQAYSSVYDACVAQAKMLRASSYYSGAWRENtSSYLDATAWLEGRYATDPTYASKLNSVISEL 164
Cdd:TIGR02541 223 GVAQKLTAKFRSYSSYEEAFSDYARLLNNNPRYEAVLQQR-SAESFARGLQRAGYATDPRYARKLLQVIQSL 293
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
30-170 |
9.82e-14 |
|
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
Pssm-ID: 411609 [Multi-domain] Cd Length: 312 Bit Score: 70.93 E-value: 9.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 30 QEIINAAVPVAN----DYGLYPSVMIAQGILESSGGQSALASNYNNIFGVK-------YTSGTPIYLPTQEYLNGTMTNV 98
Cdd:NF038016 161 AQFIAAVAPPAQqsqrATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfgspgpIAVGCRSYATFECSPTGGCFDT 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046562299 99 VEPFQAYSSVYDACVAQAKMLRASSYYSGA--WRENTSSYLDATaWLEGrYATDPTYASKLNSVISELGLSVYD 170
Cdd:NF038016 241 TATFRAYASAADSFRDHGRFLSVNSRYAPAfaYTDDPDQFAREI-HKAG-YATDPTYADKLIGLMKQYNLYQYD 312
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
194-237 |
1.24e-12 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 61.73 E-value: 1.24e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1046562299 194 TYKVQEGDSLSAIAAQYGTTVDALVSANSLENANDIHVGEVLQV 237
Cdd:cd00118 2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
193-302 |
1.40e-12 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 68.61 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 193 GTYKVQEGDSLSAIAAQYGTTVDALVSANSLEnANDIHVGEVLQVAGASTTTTTTSTNTTSNVSssstytVKSGDSLYSI 272
Cdd:PRK10783 344 RSYKVRSGDTLSGIASRLNVSTKDLQQWNNLR-GSKLKVGQTLTIGAGSSAQRLANNSDSITYR------VRKGDSLSSI 416
|
90 100 110
....*....|....*....|....*....|
gi 1046562299 273 AEQYGMTVSSLMSANGiyDVNSMLQVGQVL 302
Cdd:PRK10783 417 AKRHGVNIKDVMRWNS--DTAKNLQPGDKL 444
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
29-178 |
1.67e-12 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 67.85 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 29 VQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSAL----ASNYNNIFGVKYTS---GTPIYLPTQEYLNGTMTNVVEP 101
Cdd:PRK12713 185 VSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELrhedGSTSYNLFGIKAGAswkGKVVNVMTTEYVDGVAQKLVQP 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046562299 102 FQAYSSVYDACVAQAKMLRASSYYSGAwrENTSSYLDATAWL-EGRYATDPTYASKLNSVISELGLSVYDqgGEISGG 178
Cdd:PRK12713 265 FRAYSSYEESFSDYARLIGNSPRYEAV--TQAGNEIEAARRIqEAGYATDPRYAEKLISIMGQLRTSVAR--ADFSGG 338
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
11-160 |
2.31e-12 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 67.68 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 11 ASIVALASLGGiKAQAASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSALA--SNYNNIFGVKYT--SGTPIYLP 86
Cdd:PRK12711 202 AASTAAASLGE-RTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGngGDSNNLFGIKATgwNGDKVTTG 280
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046562299 87 TQEYLNGTMTNVVEPFQAYSSVYDACVAQAKMLRASSYYSGAWRENTSSYLDATAWLEGRYATDPTYASKLNSV 160
Cdd:PRK12711 281 THEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTDIKGFARGLQQAGYATDPGYAAKIAAI 354
|
|
| LysM |
smart00257 |
Lysin motif; |
194-237 |
9.99e-12 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 59.00 E-value: 9.99e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1046562299 194 TYKVQEGDSLSAIAAQYGTTVDALVSANSLENANDIHVGEVLQV 237
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
20-165 |
1.97e-11 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 64.17 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 20 GGIKAQAASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSAL----ASNYNNIFGVKYT---SGTPIYLPTQEYLN 92
Cdd:PRK12709 168 GGSPDADAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIrgadGSTSYNVFGIKATkgwTGRTVSAVTTEYVN 247
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046562299 93 GTMTNVVEPFQAYSSVYDACVAQAKMLRASSYYSGAWRENTSSYLDATAWLEGRYATDPTYASKLNSVISELG 165
Cdd:PRK12709 248 GKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQIG 320
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
263-303 |
4.70e-11 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 57.02 E-value: 4.70e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 263 VKSGDSLYSIAEQYGMTVSSLMSANGIYdvNSMLQVGQVLQ 303
Cdd:pfam01476 3 VKKGDTLSSIAKRYGITVEQLAELNGLS--SPNLYVGQKLK 41
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
195-237 |
6.01e-11 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 57.02 E-value: 6.01e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1046562299 195 YKVQEGDSLSAIAAQYGTTVDALVSANSLeNANDIHVGEVLQV 237
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGL-SSPNLYVGQKLKI 42
|
|
| LysM |
smart00257 |
Lysin motif; |
263-303 |
6.74e-11 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 56.69 E-value: 6.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 263 VKSGDSLYSIAEQYGMTVSSLMSANGIYDvNSMLQVGQVLQ 303
Cdd:smart00257 4 VKKGDTLSSIARRYGISVSDLLELNNILD-PDNLQVGQKLK 43
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
263-302 |
1.40e-10 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 59.34 E-value: 1.40e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1046562299 263 VKSGDSLYSIAEQYGMTVSSLMSANGIYdvNSMLQVGQVL 302
Cdd:COG1388 114 VKKGDTLWSIARRYGVSVEELKRWNGLS--SDTIRPGQKL 151
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
263-303 |
6.35e-10 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 54.03 E-value: 6.35e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 263 VKSGDSLYSIAEQYGMTVSSLMSANGIYDvNSMLQVGQVLQ 303
Cdd:cd00118 5 VKPGDTLWSIAKKYGVTVEELAAANPLIN-PDCIYPGQKLK 44
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
263-358 |
3.08e-09 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 58.21 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 263 VKSGDSLYSIAEQYGMTVSSLMSANGIYdvNSMLQVGQVLQVTVSTSATTSNTTTSNSY-TIQNGDSIYSIATANGMTAD 341
Cdd:PRK10783 348 VRSGDTLSGIASRLNVSTKDLQQWNNLR--GSKLKVGQTLTIGAGSSAQRLANNSDSITyRVRKGDSLSSIAKRHGVNIK 425
|
90
....*....|....*..
gi 1046562299 342 QLAALNGfGINDMIHPG 358
Cdd:PRK10783 426 DVMRWNS-DTAKNLQPG 441
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
323-363 |
3.11e-09 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 52.10 E-value: 3.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 323 IQNGDSIYSIATANGMTADQLAALNGFGINDMIHPGQTIRI 363
Cdd:cd00118 5 VKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
323-363 |
1.34e-08 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 50.09 E-value: 1.34e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 323 IQNGDSIYSIATANGMTADQLAALNGFGiNDMIHPGQTIRI 363
Cdd:pfam01476 3 VKKGDTLSSIAKRYGITVEQLAELNGLS-SPNLYVGQKLKI 42
|
|
| LysM |
smart00257 |
Lysin motif; |
323-363 |
5.59e-08 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 48.60 E-value: 5.59e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 323 IQNGDSIYSIATANGMTADQLAALNGFGINDMIHPGQTIRI 363
Cdd:smart00257 4 VKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
26-157 |
1.09e-07 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 53.09 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 26 AASVQEIINAAVPVANDYGLYPSVMIAQGILESSGGQSAL----ASNYNNIFGVKYTS---GTPIYLPTQEYLNGTMTNV 98
Cdd:PRK12712 198 SAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREIthadGSTTFNVFGIKAGAnwkGRVAEVTTTEYVDGQPQKV 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 99 VEPFQAYSSVYDACVAQAKMLRASSYYSGAWRENTSSylDATAWLE-GRYATDPTYASKL 157
Cdd:PRK12712 278 RARFRAYGSYDEACADYARLLTSNPRYAGVVSAASAD--EAAHGLQrAGYATDPAYGHKL 335
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
323-363 |
1.71e-07 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 50.48 E-value: 1.71e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1046562299 323 IQNGDSIYSIATANGMTADQLAALNGFGiNDMIHPGQTIRI 363
Cdd:COG1388 114 VKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLKI 153
|
|
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
44-161 |
1.71e-07 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 52.19 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 44 GLYPSVMIAQGILESSGGQS----ALASNYNNIFGVKYTS---GTPIYLPTQEYLNGTMTNVVEPFQAYSSVYDACVAQA 116
Cdd:PRK05684 171 GVPHHLLLAQAALESGWGQReirtADGSPSHNLFGIKADGswkGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYV 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1046562299 117 KMLRASSYYSgAWRENTSSYLDATAWLEGRYATDPTYASKLNSVI 161
Cdd:PRK05684 251 SLLTNNPRYA-AVTQAASPEQFARALQDAGYATDPNYARKLVSVI 294
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
29-160 |
5.03e-06 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 47.48 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046562299 29 VQEIINAAVPVANDYGLYPSVMIAQGILESSGGQ----SALASNYNNIFGVKYTSGT---PIYLPTQEYLNGTMTNVVEP 101
Cdd:PRK12710 134 VKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKfvtrDADGSSSNNLFNIKTGSHSeveSIQVKTTEYIADTPIKINAS 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046562299 102 FQAYSSVYDACVAQAKMLRASSYYSGAWRENTSSYLDATAWLEGRYATDPTYASKLNSV 160
Cdd:PRK12710 214 FRKYPSIEHSFHDYVSLIKGSERYQMALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
194-237 |
4.29e-05 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 45.46 E-value: 4.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1046562299 194 TYKVQEGDSLSAIAAQYGTTVDALVSANSLeNANDIHVGEVLQV 237
Cdd:PRK06347 549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKL-TSNMIHVGQKLTI 591
|
|
|