NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1182682411|emb|SMF04728|]
View 

peptidoglycan hydrolases with endo-beta-N-acetylglucosaminidase [Bacillus subtilis]

Protein Classification

FlgJ and GW domain-containing protein( domain architecture ID 10004352)

FlgJ and GW domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 91-258 1.84e-59

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


:

Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 192.49  E-value: 1.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  91 ATTLSKPIETSKETEEIDEQQVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL-AAKANNLFGVKGNY--KGH 167
Cdd:COG1705   110 SLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGswQGK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 168 HVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLE-AGNYKEAATALQTSGYATDPDYADK 246
Cdd:COG1705   190 SVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLK-----NNPRYAGALAnAKDYEAFAKALQKAGYATDPKYADK 264

                         170
                  ....*....|..
gi 1182682411 247 ISAIVEKYDLDE 258
Cdd:COG1705   265 LISIIESYNLTQ 276
GW pfam13457
GW (Gly-Tryp) dipeptide domain; This is a GW domain found in the C-terminal of InlB proteins ...
 267-339 4.43e-14

GW (Gly-Tryp) dipeptide domain; This is a GW domain found in the C-terminal of InlB proteins which belong to the extended family of internalin proteins found in Listeria. These 80 residue GW domains are unique to InlB among the internalins but are present in other proteins of Gram-positive bacteria. GW domains (named after a GlyTryp dipeptide) are structurally and evolutionary related to SH3 domains. Despite of this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. They are highly basic and interact with poly-anions. The GW domains are responsible for the non-covalent attachment to the bacterial cell surface through binding to lipoteichoic acid. The GW domains alone do not stimulate uptake, but they synergize with the Met-binding internalin domain.


:

Pssm-ID: 463884  Cd Length: 74  Bit Score: 66.60  E-value: 4.43e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182682411 267 KSVDLNASIKDSAVQDVWSKPSTDDRSIRLTSAQSYVGKDIKVVSKKQKGQSVWYQFQINDKLIGWIDDSAVE 339
Cdd:pfam13457   2 KNVNYTATINNSSNDGIYSKPPATTSAKKLGTTKKYNGKTVTVLKEAKTKRGTYYQITDNGKTIGWIDKRALK 74
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 91-258 1.84e-59

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 192.49  E-value: 1.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  91 ATTLSKPIETSKETEEIDEQQVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL-AAKANNLFGVKGNY--KGH 167
Cdd:COG1705   110 SLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGswQGK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 168 HVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLE-AGNYKEAATALQTSGYATDPDYADK 246
Cdd:COG1705   190 SVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLK-----NNPRYAGALAnAKDYEAFAKALQKAGYATDPKYADK 264

                         170
                  ....*....|..
gi 1182682411 247 ISAIVEKYDLDE 258
Cdd:COG1705   265 LISIIESYNLTQ 276
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 102-260 4.85e-51

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 166.46  E-value: 4.85e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  102 KETEEIDEQqVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKANNLFGVKGNYKGHHVTMETDEVEKGKR 181
Cdd:smart00047   1 KLLAGGSTL-EFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGGW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  182 KTIRAKFRKYstFFESMDDHAQLFVrgtsWNKKKYKPVLEagnykeaATALQTSGYATDPDYADKISAIVEKYD--LDEY 259
Cdd:smart00047  80 VTVKAAFRGY--FGEKFIDYAYVLR----GQNPLYKKRWG-------SNALQTAGYATDPDYAKKLIRIIALYDekLKGY 146


                   .
gi 1182682411  260 D 260
Cdd:smart00047 147 D 147
PRK08581 PRK08581
amidase domain-containing protein;
86-274 5.65e-42

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 154.18  E-value: 5.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  86 ALFVLATTLSKpIETSKETEEIDEQQV--FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKAN-NLFGVKG 162
Cdd:PRK08581  295 SLFETGPSLSN-NDDSGSFNVVDSKDTrqFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNhNLFGIKG 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 163 NYKGHHVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDHAQLFVRGTSWNKKKYKPVL--EAGNYKEAATALQTSgYATD 240
Cdd:PRK08581  374 AYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLIKNGIDGNSTIYKPTWksEAKSYKDATSHLSKT-YATD 452

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1182682411 241 PDYADKISAIVEKYDLDEYDE--------VNPSLKSVDLNAS 274
Cdd:PRK08581  453 PNYAKKLNSIIKHYNLTQFDDekmpdldkYESSIKDYDDSSS 494
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 113-260 3.10e-31

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: 119.85  E-value: 3.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKANNLFGVK--GNYKGHHV---TMETDEVEK-GKRKTIRA 186
Cdd:NF038016  163 FIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfGSPGPIAVgcrSYATFECSPtGGCFDTTA 242

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182682411 187 KFRKYSTFFESMDDHAQLFvrgtsWNKKKYKPVLE-AGNYKEAATALQTSGYATDPDYADKISAIVEKYDLDEYD 260
Cdd:NF038016  243 TFRAYASAADSFRDHGRFL-----SVNSRYAPAFAyTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 113-253 4.87e-31

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: 118.80  E-value: 4.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL----AAKANNLFGVK--GNYKGHHVTMETDEVEKGKRKTIRA 186
Cdd:TIGR02541 151 FVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTA 230

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182682411 187 KFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLEAGNYKEAATALQTSGYATDPDYADKISAIVEK 253
Cdd:TIGR02541 231 KFRSYSSYEEAFSDYARLLN-----NNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQS 292
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 120-256 6.86e-27

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: 101.50  E-value: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 120 HAQILYEKYHVLPSITIAQAILESDWGNSELAAKANNLFGVKGNYKGhHVTMETDEVekgkrkTIRAKFRKYSTFFESMD 199
Cdd:pfam01832   3 AAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKG-KVAYDTDEV------TVAARFRKYDSVEESIR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1182682411 200 DHaqlfvrgtswnkkkykpvleagnykeaatalqtsgyatdpdYADKISAIVEKYDL 256
Cdd:pfam01832  76 DY-----------------------------------------YAEKLIAIIERYNL 91
GW pfam13457
GW (Gly-Tryp) dipeptide domain; This is a GW domain found in the C-terminal of InlB proteins ...
 267-339 4.43e-14

GW (Gly-Tryp) dipeptide domain; This is a GW domain found in the C-terminal of InlB proteins which belong to the extended family of internalin proteins found in Listeria. These 80 residue GW domains are unique to InlB among the internalins but are present in other proteins of Gram-positive bacteria. GW domains (named after a GlyTryp dipeptide) are structurally and evolutionary related to SH3 domains. Despite of this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. They are highly basic and interact with poly-anions. The GW domains are responsible for the non-covalent attachment to the bacterial cell surface through binding to lipoteichoic acid. The GW domains alone do not stimulate uptake, but they synergize with the Met-binding internalin domain.


Pssm-ID: 463884  Cd Length: 74  Bit Score: 66.60  E-value: 4.43e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182682411 267 KSVDLNASIKDSAVQDVWSKPSTDDRSIRLTSAQSYVGKDIKVVSKKQKGQSVWYQFQINDKLIGWIDDSAVE 339
Cdd:pfam13457   2 KNVNYTATINNSSNDGIYSKPPATTSAKKLGTTKKYNGKTVTVLKEAKTKRGTYYQITDNGKTIGWIDKRALK 74
GW_glycos_SH3 NF033202
GW domain; The GW domain of Listeria belongs to the clan of SH3-like domains. A similar but ...
 267-341 2.22e-13

GW domain; The GW domain of Listeria belongs to the clan of SH3-like domains. A similar but broader model (PF13457) occurs in Pfam. The GW domain occurs as repeats on surface proteins of the cell-invading pathogenic bacterium Listeria monocytogenes, and is involved in binding to glycosaminoglycans. Members of this family include the GW-type internalin InlB and several paralogs.


Pssm-ID: 380204  Cd Length: 81  Bit Score: 64.55  E-value: 2.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182682411 267 KSVDLNASIKDSAVQDVWSKPSTDDRSIRLTSAQSYVGKDIKVVSKKQKGQSVWYQFQINDKLIGWIDDSAVEIK 341
Cdd:NF033202    7 KAVNLTAYVKNAKGNGIWSKPYNTDGAKKVGTLSSYKNKKLKIDREAKTEGGTWYQFKDNGKVIGWIDAKALTIF 81
 
Name Accession Description Interval E-value
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 91-258 1.84e-59

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 192.49  E-value: 1.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  91 ATTLSKPIETSKETEEIDEQQVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL-AAKANNLFGVKGNY--KGH 167
Cdd:COG1705   110 SLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSELdGSPSNNLFGIKAGGswQGK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 168 HVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLE-AGNYKEAATALQTSGYATDPDYADK 246
Cdd:COG1705   190 SVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLK-----NNPRYAGALAnAKDYEAFAKALQKAGYATDPKYADK 264

                         170
                  ....*....|..
gi 1182682411 247 ISAIVEKYDLDE 258
Cdd:COG1705   265 LISIIESYNLTQ 276
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 102-260 4.85e-51

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 166.46  E-value: 4.85e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  102 KETEEIDEQqVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKANNLFGVKGNYKGHHVTMETDEVEKGKR 181
Cdd:smart00047   1 KLLAGGSTL-EFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAKKYNNLFGIKGAYDGRPVRMGTLEYLNGGW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  182 KTIRAKFRKYstFFESMDDHAQLFVrgtsWNKKKYKPVLEagnykeaATALQTSGYATDPDYADKISAIVEKYD--LDEY 259
Cdd:smart00047  80 VTVKAAFRGY--FGEKFIDYAYVLR----GQNPLYKKRWG-------SNALQTAGYATDPDYAKKLIRIIALYDekLKGY 146


                   .
gi 1182682411  260 D 260
Cdd:smart00047 147 D 147
PRK08581 PRK08581
amidase domain-containing protein;
86-274 5.65e-42

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 154.18  E-value: 5.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  86 ALFVLATTLSKpIETSKETEEIDEQQV--FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKAN-NLFGVKG 162
Cdd:PRK08581  295 SLFETGPSLSN-NDDSGSFNVVDSKDTrqFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSPNhNLFGIKG 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 163 NYKGHHVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDHAQLFVRGTSWNKKKYKPVL--EAGNYKEAATALQTSgYATD 240
Cdd:PRK08581  374 AYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLIKNGIDGNSTIYKPTWksEAKSYKDATSHLSKT-YATD 452

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1182682411 241 PDYADKISAIVEKYDLDEYDE--------VNPSLKSVDLNAS 274
Cdd:PRK08581  453 PNYAKKLNSIIKHYNLTQFDDekmpdldkYESSIKDYDDSSS 494
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
111-265 1.82e-31

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 124.42  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 111 QVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKAN-NLFGVKGNYKGHHVTMETDEVE-KGKRKTIRAKF 188
Cdd:PRK06347  151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNyNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKF 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182682411 189 RKYSTFFESMDDHAQLFVRGTSWNKKKYKPVLEAG--NYKEAATALqTSGYATDPDYADKISAIVEKYDLDEYDEVNPS 265
Cdd:PRK06347  231 RKYPSYHQSLEDYAQVIRKGPSWNPNYYSKVWKSNttSYKDATKAL-TGTYATDTAYATKLNDLISRYNLTQYDSGKTT 308
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 113-260 3.10e-31

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: 119.85  E-value: 3.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAKANNLFGVK--GNYKGHHV---TMETDEVEK-GKRKTIRA 186
Cdd:NF038016  163 FIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTREDHNYFGIKcfGSPGPIAVgcrSYATFECSPtGGCFDTTA 242

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182682411 187 KFRKYSTFFESMDDHAQLFvrgtsWNKKKYKPVLE-AGNYKEAATALQTSGYATDPDYADKISAIVEKYDLDEYD 260
Cdd:NF038016  243 TFRAYASAADSFRDHGRFL-----SVNSRYAPAFAyTDDPDQFAREIHKAGYATDPTYADKLIGLMKQYNLYQYD 312
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 113-253 4.87e-31

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: 118.80  E-value: 4.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL----AAKANNLFGVK--GNYKGHHVTMETDEVEKGKRKTIRA 186
Cdd:TIGR02541 151 FVNSMLPHARKAAQQLGVPPHLILAQAALESGWGQRQIrnadGSPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTA 230

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182682411 187 KFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLEAGNYKEAATALQTSGYATDPDYADKISAIVEK 253
Cdd:TIGR02541 231 KFRSYSSYEEAFSDYARLLN-----NNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQS 292
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
84-253 7.75e-29

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 113.05  E-value: 7.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  84 PLALFVLATTLSKPIETSKETeeIDEQQVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAK----ANNLFG 159
Cdd:PRK05684  128 ALAQLVRKAIPQPPLASDKPL--FGSSDDFVARLSPPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTAdgspSHNLFG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 160 VK--GNYKGHHVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDhaqlFVRGTSwNKKKYKPVLEAGNYKEAATALQTSGY 237
Cdd:PRK05684  206 IKadGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFND----YVSLLT-NNPRYAAVTQAASPEQFARALQDAGY 280

                         170
                  ....*....|....*.
gi 1182682411 238 ATDPDYADKISAIVEK 253
Cdd:PRK05684  281 ATDPNYARKLVSVIQQ 296
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 120-256 6.86e-27

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: 101.50  E-value: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 120 HAQILYEKYHVLPSITIAQAILESDWGNSELAAKANNLFGVKGNYKGhHVTMETDEVekgkrkTIRAKFRKYSTFFESMD 199
Cdd:pfam01832   3 AAIEAAKKYGIPASVLLAQAALESGWGTSRLAKESNNLFGIKASWKG-KVAYDTDEV------TVAARFRKYDSVEESIR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1182682411 200 DHaqlfvrgtswnkkkykpvleagnykeaatalqtsgyatdpdYADKISAIVEKYDL 256
Cdd:pfam01832  76 DY-----------------------------------------YAEKLIAIIERYNL 91
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
113-250 4.25e-23

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 98.88  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELA--AKANNLFGVKGN-YKGHHVTMETDEVEKGKRKTIRAKFR 189
Cdd:PRK12711  218 FVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGngGDSNNLFGIKATgWNGDKVTTGTHEYVNGVKTTETADFR 297

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1182682411 190 KYSTFFESMDDHAQLFVrgtswNKKKYKPVLEAG-NYKEAATALQTSGYATDPDYADKISAI 250
Cdd:PRK12711  298 AYGSAEESFADYVRLLK-----NNSRYQQALQAGtDIKGFARGLQQAGYATDPGYAAKIAAI 354
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 113-253 1.18e-22

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 97.00  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL----AAKANNLFGVKG--NYKGHHVTMETDEVEKGKRKTIRA 186
Cdd:PRK12712  200 FVARMAGPAEAASRASGVPARLIVGQAALESGWGRREIthadGSTTFNVFGIKAgaNWKGRVAEVTTTEYVDGQPQKVRA 279

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182682411 187 KFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLEAGNYKEAATALQTSGYATDPDYADKISAIVEK 253
Cdd:PRK12712  280 RFRAYGSYDEACADYARLLT-----SNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHKLVKIMKK 341
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 113-251 5.17e-22

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 95.20  E-value: 5.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 113 FIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSEL----AAKANNLFGVKG--NYKGHHVTMETDEVEKGKRKTIRA 186
Cdd:PRK12713  184 FVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELrhedGSTSYNLFGIKAgaSWKGKVVNVMTTEYVDGVAQKLVQ 263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182682411 187 KFRKYSTFFESMDDHAQLFvrgtsWNKKKYKPVLEAGNYKEAATALQTSGYATDPDYADKISAIV 251
Cdd:PRK12713  264 PFRAYSSYEESFSDYARLI-----GNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIM 323
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 91-253 5.42e-21

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 91.91  E-value: 5.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411  91 ATTLSKPIETSKETEEIDeqqVFIDSLSGHAQILYEKYHVLPSITIAQAILESDWGNSELAAK----ANNLFGVKG--NY 164
Cdd:PRK12709  157 GSALTPPLKGNGGSPDAD---AFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGAdgstSYNVFGIKAtkGW 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 165 KGHHVTMETDEVEKGKRKTIRAKFRKYSTFFESMDDHAQLFVrgtswNKKKYKPVLEAGNYKEA-ATALQTSGYATDPDY 243
Cdd:PRK12709  234 TGRTVSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLK-----NNPRYAGVLNASRSVEGfAHGMQKAGYATDPHY 308

                         170
                  ....*....|
gi 1182682411 244 ADKISAIVEK 253
Cdd:PRK12709  309 AKKLISIMQQ 318
GW pfam13457
GW (Gly-Tryp) dipeptide domain; This is a GW domain found in the C-terminal of InlB proteins ...
 267-339 4.43e-14

GW (Gly-Tryp) dipeptide domain; This is a GW domain found in the C-terminal of InlB proteins which belong to the extended family of internalin proteins found in Listeria. These 80 residue GW domains are unique to InlB among the internalins but are present in other proteins of Gram-positive bacteria. GW domains (named after a GlyTryp dipeptide) are structurally and evolutionary related to SH3 domains. Despite of this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. They are highly basic and interact with poly-anions. The GW domains are responsible for the non-covalent attachment to the bacterial cell surface through binding to lipoteichoic acid. The GW domains alone do not stimulate uptake, but they synergize with the Met-binding internalin domain.


Pssm-ID: 463884  Cd Length: 74  Bit Score: 66.60  E-value: 4.43e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182682411 267 KSVDLNASIKDSAVQDVWSKPSTDDRSIRLTSAQSYVGKDIKVVSKKQKGQSVWYQFQINDKLIGWIDDSAVE 339
Cdd:pfam13457   2 KNVNYTATINNSSNDGIYSKPPATTSAKKLGTTKKYNGKTVTVLKEAKTKRGTYYQITDNGKTIGWIDKRALK 74
GW_glycos_SH3 NF033202
GW domain; The GW domain of Listeria belongs to the clan of SH3-like domains. A similar but ...
 267-341 2.22e-13

GW domain; The GW domain of Listeria belongs to the clan of SH3-like domains. A similar but broader model (PF13457) occurs in Pfam. The GW domain occurs as repeats on surface proteins of the cell-invading pathogenic bacterium Listeria monocytogenes, and is involved in binding to glycosaminoglycans. Members of this family include the GW-type internalin InlB and several paralogs.


Pssm-ID: 380204  Cd Length: 81  Bit Score: 64.55  E-value: 2.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182682411 267 KSVDLNASIKDSAVQDVWSKPSTDDRSIRLTSAQSYVGKDIKVVSKKQKGQSVWYQFQINDKLIGWIDDSAVEIK 341
Cdd:NF033202    7 KAVNLTAYVKNAKGNGIWSKPYNTDGAKKVGTLSSYKNKKLKIDREAKTEGGTWYQFKDNGKVIGWIDAKALTIF 81
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 132-272 3.59e-09

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 57.11  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 132 PSITIAQAILESDWGN----SELAAKANNLFGVKgnyKGHHVTMETDEVEKGKRKT-----IRAKFRKYSTFFESMDDHA 202
Cdd:PRK12710  152 PKLLVAQAALETGWGKfvtrDADGSSSNNLFNIK---TGSHSEVESIQVKTTEYIAdtpikINASFRKYPSIEHSFHDYV 228

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1182682411 203 QLfVRGTswnkKKYKPVL-EAGNYKEAATALQTSGYATDPDYADKISAIVEKydldeyDEVNPSLKSVDLN 272
Cdd:PRK12710  229 SL-IKGS----ERYQMALaNAENPEIYVSELNKAGYATDPNYSNKILSIYHG------DELNQAIQRCESS 288
Bax COG2992
Uncharacterized FlgJ-related protein [General function prediction only];
122-159 1.23e-05

Uncharacterized FlgJ-related protein [General function prediction only];


Pssm-ID: 442231  Cd Length: 253  Bit Score: 46.07  E-value: 1.23e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1182682411 122 QILYEKYHVLP-SITIAQAILESDWGNSELAAKANNLFG 159
Cdd:COG2992   110 EELLKRVDIIPpSLVLAQAANESGWGTSRFAREGNNLFG 148
PRK10356 PRK10356
protein bax;
124-207 1.55e-04

protein bax;


Pssm-ID: 182404  Cd Length: 274  Bit Score: 42.94  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682411 124 LYEKYHVLPSITIA-QAILESDWGNSELAAKANNLFGVKgnykghhvtmetdeVEKGKRKTIRAKFRKYSTfFESMDDHA 202
Cdd:PRK10356  142 LLERVDIIPTSMVAtMAAAESGWGTSKLARNNNNLFGMK--------------CMKGRCTNAPGKVKGYSQ-FSSVKESV 206


                  ....*
gi 1182682411 203 QLFVR 207
Cdd:PRK10356  207 SAYVT 211
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH