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Conserved domains on  [gi|1812594798|ref|WP_162844339|]
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flagellar assembly peptidoglycan hydrolase FlgJ [Enterobacillus tribolii]

Protein Classification

flagellar assembly peptidoglycan hydrolase FlgJ( domain architecture ID 11481497)

flagellar assembly peptidoglycan hydrolase FlgJ acts as a flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
27-315 3.59e-160

flagellar assembly peptidoglycan hydrolase FlgJ;


:

Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 449.33  E-value: 3.59e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  27 KRQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSGA 105
Cdd:PRK05684   21 KAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQLSaGGGLGLADMMVKQLSPE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 106 GTRLP-ESVGTVPMALDGEMMQSLPTQALEQVLRRAVPRPQRLSIPPQPG-NGDFIARLSVPAQIAGRQSGIPHQLIMAQ 183
Cdd:PRK05684  101 QSPAPeESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGsSDDFVARLSPPAQKAAQQSGVPHHLLLAQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 184 AALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYA 263
Cdd:PRK05684  181 AALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1812594798 264 QVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQIRGVGEQVVSAYTTDL 315
Cdd:PRK05684  261 AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
 
Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
27-315 3.59e-160

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 449.33  E-value: 3.59e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  27 KRQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSGA 105
Cdd:PRK05684   21 KAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQLSaGGGLGLADMMVKQLSPE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 106 GTRLP-ESVGTVPMALDGEMMQSLPTQALEQVLRRAVPRPQRLSIPPQPG-NGDFIARLSVPAQIAGRQSGIPHQLIMAQ 183
Cdd:PRK05684  101 QSPAPeESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGsSDDFVARLSPPAQKAAQQSGVPHHLLLAQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 184 AALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYA 263
Cdd:PRK05684  181 AALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1812594798 264 QVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQIRGVGEQVVSAYTTDL 315
Cdd:PRK05684  261 AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 28-301 2.05e-103

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: 304.85  E-value: 2.05e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  28 RQSAKGDGQ-SLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSGA 105
Cdd:TIGR02541  12 KAKAVKDPKeQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSaNGGIGLADMIVAQLTKG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 106 GTRLPES---VGTVPMALdgEMMQSLPT------QALEQVLRRAVPRpQRLSIPPQPG-NGDFIARLSVPAQIAGRQSGI 175
Cdd:TIGR02541  92 QGNEPSEgaaRGAAPSPL--VYRPRLDPkprrivKALIESVELSRPR-GRSHAESVPGhPKSFVNSMLPHARKAAQQLGV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 176 PHQLIMAQAALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQL 255
Cdd:TIGR02541 169 PPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARL 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1812594798 256 LTRNPRYAQVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQIR 301
Cdd:TIGR02541 249 LNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 28-300 2.05e-77

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 237.94  E-value: 2.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  28 RQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMSGKGLGIADMLVKQLSGAGT 107
Cdd:COG1705     2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 108 RLPESVGTVPMALDGEMMQSLPTQALEQVLRRAVPRPQRLSIPPQPGNGDFIARLSVPAQIAGRQSGIPHQLIMAQAALE 187
Cdd:COG1705    82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 188 SGWGEREIPAAggmRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYAQV-S 266
Cdd:COG1705   162 SGWGKSELDGS---PSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGAlA 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1812594798 267 NAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQI 300
Cdd:COG1705   239 NAKDYEAFAKALQKAGYATDPKYADKLISIIESY 272
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 157-304 1.33e-35

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 126.01  E-value: 1.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  157 DFIARLSVPAQIAGRQSGIPHQLIMAQAALESGWGEREIPAaggmRSHNLFGIKAGsrWNGPTTEITTTEYSNGVAYKTK 236
Cdd:smart00047  10 EFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIKGA--YDGRPVRMGTLEYLNGGWVTVK 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812594798  237 AKFRVYDSYLSAIRDYVqLLTRNPRYAQVSNAGspeqaahALQKAGYATDPNYAEKLVRIMNQIRGVG 304
Cdd:smart00047  84 AAFRGYFGEKFIDYAYV-LRGQNPLYKKRWGSN-------ALQTAGYATDPDYAKKLIRIIALYDEKL 143
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 151-299 3.44e-34

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: 127.16  E-value: 3.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 151 PQPGNGDFIARLSVPAQIAGRQSGIPHQLIMAQAALESGWGEreipAAGGMRSHNLFGIKA----GSRWNGPTTeITTTE 226
Cdd:NF038016  156 PRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGR----SGLTREDHNYFGIKCfgspGPIAVGCRS-YATFE 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812594798 227 YS-NGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYAQVSN-AGSPEQAAHALQKAGYATDPNYAEKLVRIMNQ 299
Cdd:NF038016  231 CSpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAyTDDPDQFAREIHKAGYATDPTYADKLIGLMKQ 305
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 166-301 2.72e-21

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: 86.47  E-value: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 166 AQIAGRQSGIPHQLIMAQAALESGWGEREIpaagGMRSHNLFGIKAGsrWNGPTTeITTTEysngvaYKTKAKFRVYDSY 245
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRL----AKESNNLFGIKAS--WKGKVA-YDTDE------VTVAARFRKYDSV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812594798 246 LSAIRDYvqlltrnpryaqvsnagspeqaahalqkagyatdpnYAEKLVRIMNQIR 301
Cdd:pfam01832  71 EESIRDY------------------------------------YAEKLIAIIERYN 90
 
Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
27-315 3.59e-160

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 449.33  E-value: 3.59e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  27 KRQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSGA 105
Cdd:PRK05684   21 KAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQLSaGGGLGLADMMVKQLSPE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 106 GTRLP-ESVGTVPMALDGEMMQSLPTQALEQVLRRAVPRPQRLSIPPQPG-NGDFIARLSVPAQIAGRQSGIPHQLIMAQ 183
Cdd:PRK05684  101 QSPAPeESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGsSDDFVARLSPPAQKAAQQSGVPHHLLLAQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 184 AALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYA 263
Cdd:PRK05684  181 AALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNPRYA 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1812594798 264 QVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQIRGVGEQVVSAYTTDL 315
Cdd:PRK05684  261 AVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 28-301 2.05e-103

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: 304.85  E-value: 2.05e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  28 RQSAKGDGQ-SLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSGA 105
Cdd:TIGR02541  12 KAKAVKDPKeQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSaNGGIGLADMIVAQLTKG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 106 GTRLPES---VGTVPMALdgEMMQSLPT------QALEQVLRRAVPRpQRLSIPPQPG-NGDFIARLSVPAQIAGRQSGI 175
Cdd:TIGR02541  92 QGNEPSEgaaRGAAPSPL--VYRPRLDPkprrivKALIESVELSRPR-GRSHAESVPGhPKSFVNSMLPHARKAAQQLGV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 176 PHQLIMAQAALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQL 255
Cdd:TIGR02541 169 PPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSYEEAFSDYARL 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1812594798 256 LTRNPRYAQVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQIR 301
Cdd:TIGR02541 249 LNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 28-300 8.79e-90

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 271.88  E-value: 8.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  28 RQSAKG--DGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMSGKGLGIADMLVKQLSGA 105
Cdd:PRK12712   27 KHSARGgaDAGTLQAAARQFEAVFTQMVLKSMRDATPQDGLFDNEQSKLYMSMMDQQLAQQMSSRGIGLADVMVRQLARA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 106 -GTRLPESVGTVP-----MALDGEMMQSLPTQALEQVLRRAVPRPQRLSIPPQP-------------------GNGD--- 157
Cdd:PRK12712  107 tGTQMPPGMNAAGgatagSAADAEMARLLDGRGAGAADADAGDLPAIGTIVPGQawnptaglrqyqpqayadqGQGEdrl 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 158 -------------FIARLSVPAQIAGRQSGIPHQLIMAQAALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITT 224
Cdd:PRK12712  187 grlpddapahvsaFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKAGANWKGRVAEVTT 266

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812594798 225 TEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYAQVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQI 300
Cdd:PRK12712  267 TEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHKLVKIMKKV 342
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 27-300 2.50e-82

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 251.77  E-value: 2.50e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  27 KRQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMSGKGLGIADMLVKQL---S 103
Cdd:PRK12709   25 RAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTSKMYTSMLDQQLAQQMSSKGIGVADALMKQLlrnA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 104 GAGTRLPESVGTVPMALDGEMMQSLptqALEQVLRRAVPRPQ---RLSI-----------PPQPGNGD------FIARLS 163
Cdd:PRK12709  105 GVAAGAQGDAGAGGMGGLGGNEGGL---AAMNALAKAYANAAnngALAGtrgysagsaltPPLKGNGGspdadaFVDKLA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 164 VPAQIAGRQSGIPHQLIMAQAALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYD 243
Cdd:PRK12709  182 APAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVNGKPRRVVAKFRAYD 261

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1812594798 244 SYLSAIRDYVQLLTRNPRYAQVSNAG-SPEQAAHALQKAGYATDPNYAEKLVRIMNQI 300
Cdd:PRK12709  262 SYEHAMTDYANLLKNNPRYAGVLNASrSVEGFAHGMQKAGYATDPHYAKKLISIMQQI 319
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 28-300 2.05e-77

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


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 237.94  E-value: 2.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  28 RQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMSGKGLGIADMLVKQLSGAGT 107
Cdd:COG1705     2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 108 RLPESVGTVPMALDGEMMQSLPTQALEQVLRRAVPRPQRLSIPPQPGNGDFIARLSVPAQIAGRQSGIPHQLIMAQAALE 187
Cdd:COG1705    82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 188 SGWGEREIPAAggmRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYAQV-S 266
Cdd:COG1705   162 SGWGKSELDGS---PSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGAlA 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1812594798 267 NAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQI 300
Cdd:COG1705   239 NAKDYEAFAKALQKAGYATDPKYADKLISIIESY 272
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 31-301 6.23e-73

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 228.48  E-value: 6.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  31 AKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMSGKGLGIADMLVKQLSGAGTRLP 110
Cdd:PRK12713   32 APDGQRQQTEVARQFEALFLQMMLKRMREATPKEGLFDSQQTEMLQGMADEQLALQLASPGIGLAQALLGQMQQGQPPVP 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 111 ES-------------VGTV---PMALD--GEMMQSLPT-----QALEQVLRRAVPRPQRLSIPPQPGNG--DFIARLSVP 165
Cdd:PRK12713  112 AAaaaggdaaaaralAGTAapaPLVRDlrGNYVQPDPAprrevNALLDVLRSNRARDRAMAAAEGAPSHvvDFVSRMSRA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 166 AQIAGRQSGIPHQLIMAQAALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSY 245
Cdd:PRK12713  192 ANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTEYVDGVAQKLVQPFRAYSSY 271

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812594798 246 LSAIRDYVQLLTRNPRYAQVSNAGSPEQAAHALQKAGYATDPNYAEKLVRIMNQIR 301
Cdd:PRK12713  272 EESFSDYARLIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLR 327
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
30-298 9.27e-43

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 151.65  E-value: 9.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  30 SAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSdQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSG---- 104
Cdd:PRK12711   13 STKADPAKIDKVSRQLEGQFAQMLVKSMRDASSGDPMFPG-ENQMFREMYDQQMAKALTdGKGLGLSAMISKQLSGdtgg 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 105 ------------------------AGTRLP------ESVGTVPMALDGEMMQSLPTQALEQVLRRAVPRP---------- 144
Cdd:PRK12711   92 palntalntakaakayslvagkrdASLPLPardgaaAGITTSSVAAAALSAGNLSGIGMSQVLDLIAGRTgageagsdda 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 145 QRLSIPP--------QPGNG-------------------------DFIARLSVPAQIAGRQSGIPHQLIMAQAALESGWG 191
Cdd:PRK12711  172 AALSWPSandrwsdvAASDAadanaavnasaastaaaslgertpeGFVAKIWTHAQKAARELGVDPRALVAQAALETGWG 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 192 EREIpaAGGMRSHNLFGIKAgSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYAQVSNAGSP 271
Cdd:PRK12711  252 RRGI--GNGGDSNNLFGIKA-TGWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTD 328

                         330       340
                  ....*....|....*....|....*...
gi 1812594798 272 EQA-AHALQKAGYATDPNYAEKLVRIMN 298
Cdd:PRK12711  329 IKGfARGLQQAGYATDPGYAAKIAAIAN 356
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 27-296 2.72e-36

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 132.22  E-value: 2.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  27 KRQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAA---LPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQL 102
Cdd:PRK12710   18 KVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGqhfLDESSPFSGKNEATFQEMLDTQYASTIAeSKGIGLAALLAKQL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 103 SgagtrlpESVGTVPMALDGEMMQSLPTQALEQvlrravprPQRLSIPpqpgnGDFIARLSVPAQIAGRQSGIPHQLIMA 182
Cdd:PRK12710   98 E-------NSVGDKANNPVNSSTEVSNTKVTNS--------EESLSVV-----DDFVKSVWPTAKQAASLIGLDPKLLVA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 183 QAALESGWGEREIPAAGGMRSHNLFGIKAGSRWNGPTTEITTTEYSNGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRY 262
Cdd:PRK12710  158 QAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKINASFRKYPSIEHSFHDYVSLIKGSERY 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1812594798 263 AQ-VSNAGSPEQAAHALQKAGYATDPNYAEKLVRI 296
Cdd:PRK12710  238 QMaLANAENPEIYVSELNKAGYATDPNYSNKILSI 272
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 157-304 1.33e-35

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


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 126.01  E-value: 1.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  157 DFIARLSVPAQIAGRQSGIPHQLIMAQAALESGWGEREIPAaggmRSHNLFGIKAGsrWNGPTTEITTTEYSNGVAYKTK 236
Cdd:smart00047  10 EFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIKGA--YDGRPVRMGTLEYLNGGWVTVK 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812594798  237 AKFRVYDSYLSAIRDYVqLLTRNPRYAQVSNAGspeqaahALQKAGYATDPNYAEKLVRIMNQIRGVG 304
Cdd:smart00047  84 AAFRGYFGEKFIDYAYV-LRGQNPLYKKRWGSN-------ALQTAGYATDPDYAKKLIRIIALYDEKL 143
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 151-299 3.44e-34

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: 127.16  E-value: 3.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 151 PQPGNGDFIARLSVPAQIAGRQSGIPHQLIMAQAALESGWGEreipAAGGMRSHNLFGIKA----GSRWNGPTTeITTTE 226
Cdd:NF038016  156 PRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGR----SGLTREDHNYFGIKCfgspGPIAVGCRS-YATFE 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812594798 227 YS-NGVAYKTKAKFRVYDSYLSAIRDYVQLLTRNPRYAQVSN-AGSPEQAAHALQKAGYATDPNYAEKLVRIMNQ 299
Cdd:NF038016  231 CSpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPAFAyTDDPDQFAREIHKAGYATDPTYADKLIGLMKQ 305
FlgJ1 COG3951
Rod binding protein domain [Cell motility];
27-105 7.62e-32

Rod binding protein domain [Cell motility];


Pssm-ID: 443151 [Multi-domain]  Cd Length: 107  Bit Score: 114.63  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  27 KRQSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAALPQDGILSSDQTRLYTSLYDQQIAQAMS-GKGLGIADMLVKQLSGA 105
Cdd:COG3951    22 KAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMFRDMLDQQLAKELAkGGGLGLADMIYRQLSRQ 101
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 166-301 2.72e-21

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: 86.47  E-value: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 166 AQIAGRQSGIPHQLIMAQAALESGWGEREIpaagGMRSHNLFGIKAGsrWNGPTTeITTTEysngvaYKTKAKFRVYDSY 245
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRL----AKESNNLFGIKAS--WKGKVA-YDTDE------VTVAARFRKYDSV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812594798 246 LSAIRDYvqlltrnpryaqvsnagspeqaahalqkagyatdpnYAEKLVRIMNQIR 301
Cdd:pfam01832  71 EESIRDY------------------------------------YAEKLIAIIERYN 90
PRK08581 PRK08581
amidase domain-containing protein;
157-298 7.46e-20

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 89.85  E-value: 7.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 157 DFIARLSVPAQIAGRQSGIPHQLIMAQAALESGWGEREIPAAGgmrSHNLFGIKaGSrWNGPTTEITTTEYSNGVAYKTK 236
Cdd:PRK08581  322 QFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKSP---NHNLFGIK-GA-YEGNSVSFNTLEADGNQLYSIN 396

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812594798 237 AKFRVYDSYLSAIRDYVQLL----TRNPR-YAQV--SNAGSPEQAAHALQKAgYATDPNYAEKLVRIMN 298
Cdd:PRK08581  397 AGFRKYPSTKESLEDYADLIkngiDGNSTiYKPTwkSEAKSYKDATSHLSKT-YATDPNYAKKLNSIIK 464
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
166-293 4.42e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 75.89  E-value: 4.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 166 AQIAGrQSGIPHQLIMAQAALESGWGEREIpaaGGMRSHNLFGIKAGsrWNGPT-TEITTTEYSNGVAYKTKAKFRVYDS 244
Cdd:PRK06347  162 SQIAA-ENDLYASVMIAQAILESAYGTSEL---GSAPNYNLFGIKGA--YNGQSyTKQTLEDDGKGNYYTITAKFRKYPS 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1812594798 245 YLSAIRDYVQLLTRNPR-----YAQV--SNAGSPEQAAHALqKAGYATDPNYAEKL 293
Cdd:PRK06347  236 YHQSLEDYAQVIRKGPSwnpnyYSKVwkSNTTSYKDATKAL-TGTYATDTAYATKL 290
flgJ PRK12708
peptidoglycan hydrolase; Reviewed
 29-126 3.09e-12

peptidoglycan hydrolase; Reviewed


Pssm-ID: 139168 [Multi-domain]  Cd Length: 134  Bit Score: 62.93  E-value: 3.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798  29 QSAKGDGQSLRQVAQQMEGLFVQMMLKSMRAA----LPQDGILSSDQTRLYTSLYDQQIAQAMSG-KGLGIADMLVKQLS 103
Cdd:PRK12708   19 IPQNLEQGALKLAAQQFEAQFLQTVLKQMRSAsdvmADEDDPFNSKNQGMYRDFYDAELASRLSSqRSMGLAEVMIKQLS 98

                          90       100
                  ....*....|....*....|...
gi 1812594798 104 GAGTRLPESVGTVPMALDGEMMQ 126
Cdd:PRK12708   99 SKLKSAPEVVALESQTLTTTAMQ 121
Rod-binding pfam10135
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ...
 55-101 5.54e-11

Rod binding protein; Members of this family are involved in the assembly of the prokaryotic flagellar rod.


Pssm-ID: 431078 [Multi-domain]  Cd Length: 50  Bit Score: 56.83  E-value: 5.54e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1812594798  55 KSMRAALPQDGIL--SSDQTRLYTSLYDQQIAQAMSGK-GLGIADMLVKQ 101
Cdd:pfam10135   1 KSMRKTVPKEDGLfdGSEAEDMFRDMLDQQLAKQLAKGgGLGLADMLYRQ 50
Bax COG2992
Uncharacterized FlgJ-related protein [General function prediction only];
175-264 1.74e-06

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


Pssm-ID: 442231  Cd Length: 253  Bit Score: 48.38  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812594798 175 IPHQLIMAQAALESGWGE----REipaaggmrSHNLFGIKAGSRWNGptteITTTEYSNGVAYktkaKFRVYDSYLSAIR 250
Cdd:COG2992   119 IPPSLVLAQAANESGWGTsrfaRE--------GNNLFGQWCFSKGCG----LVPKQRDEGANH----EVAKFDSPQASVR 182

                          90
                  ....*....|....
gi 1812594798 251 DYVQLLTRNPRYAQ 264
Cdd:COG2992   183 SYMLNLNTHPAYKD 196
 
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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