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Conserved domains on  [gi|1046562299|emb|SBW29747|]
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N-acetylmuramidase [Lactococcus lactis subsp. lactis]

Protein Classification

glycoside hydrolase family 73 protein( domain architecture ID 12811019)

glycoside hydrolase family 73 protein similar to Listeria monocytogenes virulence-associated peptidoglycan hydrolase Auto and Leuconostoc citreum atypical peptidoglycan hydrolase Mur

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
27-363 1.05e-40

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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