|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
1-309 |
0e+00 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 522.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 1 MSDLMAMSGAAYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQ 80
Cdd:PRK05684 1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 81 MSA-KGLGLADMMVEQLSGSTSP--SETAGTVPMMLDNEVLQTLPAQALAQMVRRAMPTPPTNNSAPLPQGTGNFVARMS 157
Cdd:PRK05684 81 LSAgGGLGLADMMVKQLSPEQSPapEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGSSDDFVARLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 158 IPAQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYG 237
Cdd:PRK05684 161 PPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696331843 238 SYVEAVTDYVKLLTQNPRYANVAAARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMKNTGEQAVKAYSSDL 309
Cdd:PRK05684 241 SYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
10-295 |
3.14e-116 |
|
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: 336.82 E-value: 3.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 10 AAYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSA-KGLGL 88
Cdd:TIGR02541 1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSAnGGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 89 ADMMVEQLSgSTSPSETAGTVPMMLDNEVLQTLPA---------QALAQMVRRAMPTPPTNNSApLPQGTGNFVARMSIP 159
Cdd:TIGR02541 81 ADMIVAQLT-KGQGNEPSEGAARGAAPSPLVYRPRldpkprrivKALIESVELSRPRGRSHAES-VPGHPKSFVNSMLPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 160 AQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYGSY 239
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 696331843 240 VEAVTDYVKLLTQNPRYANVAAARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMK 295
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
22-297 |
4.24e-70 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 219.07 E-value: 4.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 22 RDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSAKGLGLADMMVEQLSGSTS 101
Cdd:COG1705 2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 102 PSETAGTVPMMLDNEVLQTLPAQALAQMVRRAMPTPPTNNSAPLPQGTGNFVARMSIPAQIASQQSGIPHQLIVAQAALE 181
Cdd:COG1705 82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 182 SGWGQREIptaDGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYANV-A 260
Cdd:COG1705 162 SGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGAlA 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 696331843 261 AARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMKNT 297
Cdd:COG1705 239 NAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLT 275
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
144-298 |
3.62e-39 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 134.87 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 144 PLPQGTGNFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIptadGKTSYNVFGIKAgsNWDGPVSEITTTEYEQ 223
Cdd:smart00047 3 LAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKL----AKKYNNLFGIKG--AYDGRPVRMGTLEYLN 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696331843 224 GVAKKTKARFRVYGSYVEAVTDYVkLLTQNPRYANVaaarspeQGAHALQQAGYATDPQYAQKLVSVIQQMKNTG 298
Cdd:smart00047 77 GGWVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKR-------WGSNALQTAGYATDPDYAKKLIRIIALYDEKL 143
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
127-293 |
7.81e-26 |
|
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: 104.44 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 127 AQMVRRAMPTPPTNNSAPLPQGT-GNFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQreipTADGKTSYNVFGIKA 205
Cdd:NF038016 137 AAYVRRPWLPWCGQDPPTVPRGTpAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGR----SGLTREDHNYFGIKC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 206 gSNWDGPV----SEITTTEYEQ-GVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYAN-VAAARSPEQGAHALQQAGYAT 279
Cdd:NF038016 213 -FGSPGPIavgcRSYATFECSPtGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPaFAYTDDPDQFAREIHKAGYAT 291
|
170
....*....|....
gi 696331843 280 DPQYAQKLVSVIQQ 293
Cdd:NF038016 292 DPTYADKLIGLMKQ 305
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
160-295 |
1.00e-20 |
|
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: 84.55 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 160 AQIASQQSGIPHQLIVAQAALESGWGQreipTADGKTSYNVFGIKAGsnWDGPVSeITTTEYeqgvakKTKARFRVYGSY 239
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGT----SRLAKESNNLFGIKAS--WKGKVA-YDTDEV------TVAARFRKYDSV 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 696331843 240 VEAVTDYvklltqnpryanvaaarspeqgahalqqagyatdpqYAQKLVSVIQQMK 295
Cdd:pfam01832 71 EESIRDY------------------------------------YAEKLIAIIERYN 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
1-309 |
0e+00 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 522.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 1 MSDLMAMSGAAYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQ 80
Cdd:PRK05684 1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 81 MSA-KGLGLADMMVEQLSGSTSP--SETAGTVPMMLDNEVLQTLPAQALAQMVRRAMPTPPTNNSAPLPQGTGNFVARMS 157
Cdd:PRK05684 81 LSAgGGLGLADMMVKQLSPEQSPapEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGSSDDFVARLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 158 IPAQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYG 237
Cdd:PRK05684 161 PPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696331843 238 SYVEAVTDYVKLLTQNPRYANVAAARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMKNTGEQAVKAYSSDL 309
Cdd:PRK05684 241 SYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
10-295 |
3.14e-116 |
|
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: 336.82 E-value: 3.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 10 AAYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSA-KGLGL 88
Cdd:TIGR02541 1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSAnGGIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 89 ADMMVEQLSgSTSPSETAGTVPMMLDNEVLQTLPA---------QALAQMVRRAMPTPPTNNSApLPQGTGNFVARMSIP 159
Cdd:TIGR02541 81 ADMIVAQLT-KGQGNEPSEGAARGAAPSPLVYRPRldpkprrivKALIESVELSRPRGRSHAES-VPGHPKSFVNSMLPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 160 AQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYGSY 239
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 696331843 240 VEAVTDYVKLLTQNPRYANVAAARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMK 295
Cdd:TIGR02541 239 EEAFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-294 |
2.73e-95 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 285.75 E-value: 2.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 11 AYDAQSLNTLKRDA-ARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSAKGLGLA 89
Cdd:PRK12712 17 ALDTQGFEALKHSArGGADAGTLQAAARQFEAVFTQMVLKSMRDATPQDGLFDNEQSKLYMSMMDQQLAQQMSSRGIGLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 90 DMMVEQL---------------SGSTSPSETAGTVPMMLDNEVLQTLPAQAL-AQMVRRAMPTPPTNNSAPLPQ------ 147
Cdd:PRK12712 97 DVMVRQLaratgtqmppgmnaaGGATAGSAADAEMARLLDGRGAGAADADAGdLPAIGTIVPGQAWNPTAGLRQyqpqay 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 148 -GTGN------------------FVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSN 208
Cdd:PRK12712 177 aDQGQgedrlgrlpddapahvsaFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKAGAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 209 WDGPVSEITTTEYEQGVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYANVAAARSPEQGAHALQQAGYATDPQYAQKLV 288
Cdd:PRK12712 257 WKGRVAEVTTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHKLV 336
|
....*.
gi 696331843 289 SVIQQM 294
Cdd:PRK12712 337 KIMKKV 342
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
11-294 |
1.09e-87 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 265.25 E-value: 1.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 11 AYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSAKGLGLAD 90
Cdd:PRK12709 15 ALDVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTSKMYTSMLDQQLAQQMSSKGIGVAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 91 MMVEQL-----SGSTSPSETAGTVPMMLDNEVLQTLPAQALAQMVRRAMP----------------TPPTNNSAPLPQGT 149
Cdd:PRK12709 95 ALMKQLlrnagVAAGAQGDAGAGGMGGLGGNEGGLAAMNALAKAYANAANngalagtrgysagsalTPPLKGNGGSPDAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 150 GnFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKT 229
Cdd:PRK12709 175 A-FVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVNGKPRRV 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696331843 230 KARFRVYGSYVEAVTDYVKLLTQNPRYANV-AAARSPEQGAHALQQAGYATDPQYAQKLVSVIQQM 294
Cdd:PRK12709 254 VAKFRAYDSYEHAMTDYANLLKNNPRYAGVlNASRSVEGFAHGMQKAGYATDPHYAKKLISIMQQI 319
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
10-301 |
7.89e-79 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 243.50 E-value: 7.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 10 AAYDAQSLNTLKRDAARDPQGNLRQ--VAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSAKGLG 87
Cdd:PRK12713 15 SVFDLGRLADLKRDAVKAPDGQRQQteVARQFEALFLQMMLKRMREATPKEGLFDSQQTEMLQGMADEQLALQLASPGIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 88 LADMMVEQLSGSTSPSE-----------------TAGTVPMMLD--NEVLQTLPA-----QALAQMVRRAMPTPPTNNSA 143
Cdd:PRK12713 95 LAQALLGQMQQGQPPVPaaaaaggdaaaaralagTAAPAPLVRDlrGNYVQPDPAprrevNALLDVLRSNRARDRAMAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 144 P-LPQGTGNFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYE 222
Cdd:PRK12713 175 EgAPSHVVDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTEYV 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 696331843 223 QGVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYANVAAARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMKNTGEQA 301
Cdd:PRK12713 255 DGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRTSVARA 333
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
22-297 |
4.24e-70 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 219.07 E-value: 4.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 22 RDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQQMSAKGLGLADMMVEQLSGSTS 101
Cdd:COG1705 2 ASLDSSSASSSAGAAAQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 102 PSETAGTVPMMLDNEVLQTLPAQALAQMVRRAMPTPPTNNSAPLPQGTGNFVARMSIPAQIASQQSGIPHQLIVAQAALE 181
Cdd:COG1705 82 SAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 182 SGWGQREIptaDGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYANV-A 260
Cdd:COG1705 162 SGWGKSEL---DGSPSNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAGAlA 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 696331843 261 AARSPEQGAHALQQAGYATDPQYAQKLVSVIQQMKNT 297
Cdd:COG1705 239 NAKDYEAFAKALQKAGYATDPKYADKLISIIESYNLT 275
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
34-313 |
2.28e-39 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 142.41 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 34 QVAQQVEGMFVQMMLKSMRSALPQDGvMNSDQTRLYTSMYDQQVAQQMS-AKGLGLADMMVEQLSGST---------SPS 103
Cdd:PRK12711 23 KVSRQLEGQFAQMLVKSMRDASSGDP-MFPGENQMFREMYDQQMAKALTdGKGLGLSAMISKQLSGDTggpalntalNTA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 104 ETA---------GTVPMMLDNE-------VLQTLPA--------------QALAQMVRRAMPTPPT-------------- 139
Cdd:PRK12711 102 KAAkayslvagkRDASLPLPARdgaaagiTTSSVAAaalsagnlsgigmsQVLDLIAGRTGAGEAGsddaaalswpsand 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 140 --NNSAPLPQGTGN----------------------FVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIptADGK 195
Cdd:PRK12711 182 rwSDVAASDAADANaavnasaastaaaslgertpegFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGI--GNGG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 196 TSYNVFGIKAgSNWDGPVSEITTTEYEQGVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYANVAAARSPEQG-AHALQQ 274
Cdd:PRK12711 260 DSNNLFGIKA-TGWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQALQAGTDIKGfARGLQQ 338
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 696331843 275 AGYATDPQYAQKLVSVIQqmKNTGEQAVKAY---SSDLSQLF 313
Cdd:PRK12711 339 AGYATDPGYAAKIAAIAN--GPTIDRAVAAIgnaAADLSNRY 378
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
144-298 |
3.62e-39 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 134.87 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 144 PLPQGTGNFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIptadGKTSYNVFGIKAgsNWDGPVSEITTTEYEQ 223
Cdd:smart00047 3 LAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKL----AKKYNNLFGIKG--AYDGRPVRMGTLEYLN 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696331843 224 GVAKKTKARFRVYGSYVEAVTDYVkLLTQNPRYANVaaarspeQGAHALQQAGYATDPQYAQKLVSVIQQMKNTG 298
Cdd:smart00047 77 GGWVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKR-------WGSNALQTAGYATDPDYAKKLIRIIALYDEKL 143
|
|
| FlgJ1 |
COG3951 |
Rod binding protein domain [Cell motility]; |
1-105 |
5.78e-37 |
|
Rod binding protein domain [Cell motility];
Pssm-ID: 443151 [Multi-domain] Cd Length: 107 Bit Score: 127.73 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 1 MSDLM-AMSGAAYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSALPQDGVMNSDQTRLYTSMYDQQVAQ 79
Cdd:COG3951 1 MSISSsLSSSLALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMFRDMLDQQLAK 80
|
90 100
....*....|....*....|....*..
gi 696331843 80 QMS-AKGLGLADMMVEQLSGSTSPSET 105
Cdd:COG3951 81 ELAkGGGLGLADMIYRQLSRQQEAAAA 107
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
8-290 |
4.85e-34 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 126.06 E-value: 4.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 8 SGAAYDAQSLNTLKRDAARDPQGNLRQVAQQVEGMFVQMMLKSMRSA---LPQDGVMNSDQTRLYTSMYDQQVAQQMS-A 83
Cdd:PRK12710 5 SIATSDFQGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGqhfLDESSPFSGKNEATFQEMLDTQYASTIAeS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 84 KGLGLADMMVEQLSGSTSPSetagtvpmmldnevlqtlpAQALAQMVRRAMPTPPTNNSAPLPQgTGNFVARMSIPAQIA 163
Cdd:PRK12710 85 KGIGLAALLAKQLENSVGDK-------------------ANNPVNSSTEVSNTKVTNSEESLSV-VDDFVKSVWPTAKQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 164 SQQSGIPHQLIVAQAALESGWGQREIPTADGKTSYNVFGIKAGSNWDGPVSEITTTEYEQGVAKKTKARFRVYGSYVEAV 243
Cdd:PRK12710 145 ASLIGLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKINASFRKYPSIEHSF 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 696331843 244 TDYVKLLTQNPRYA-NVAAARSPEQGAHALQQAGYATDPQYAQKLVSV 290
Cdd:PRK12710 225 HDYVSLIKGSERYQmALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
127-293 |
7.81e-26 |
|
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: 104.44 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 127 AQMVRRAMPTPPTNNSAPLPQGT-GNFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQreipTADGKTSYNVFGIKA 205
Cdd:NF038016 137 AAYVRRPWLPWCGQDPPTVPRGTpAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGR----SGLTREDHNYFGIKC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 206 gSNWDGPV----SEITTTEYEQ-GVAKKTKARFRVYGSYVEAVTDYVKLLTQNPRYAN-VAAARSPEQGAHALQQAGYAT 279
Cdd:NF038016 213 -FGSPGPIavgcRSYATFECSPtGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYAPaFAYTDDPDQFAREIHKAGYAT 291
|
170
....*....|....
gi 696331843 280 DPQYAQKLVSVIQQ 293
Cdd:NF038016 292 DPTYADKLIGLMKQ 305
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
160-295 |
1.00e-20 |
|
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: 84.55 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 160 AQIASQQSGIPHQLIVAQAALESGWGQreipTADGKTSYNVFGIKAGsnWDGPVSeITTTEYeqgvakKTKARFRVYGSY 239
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGT----SRLAKESNNLFGIKAS--WKGKVA-YDTDEV------TVAARFRKYDSV 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 696331843 240 VEAVTDYvklltqnpryanvaaarspeqgahalqqagyatdpqYAQKLVSVIQQMK 295
Cdd:pfam01832 71 EESIRDY------------------------------------YAEKLIAIIERYN 90
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
147-292 |
7.50e-15 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 74.82 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 147 QGTGNFVARMSIPAQIASQQSGIPHQLIVAQAALESGWGQREIPTAdgkTSYNVFGIKaGSnWDGPVSEITTTEYEQGVA 226
Cdd:PRK08581 318 KDTRQFIKSIAKDAHRIGQDNDIYASVMIAQAILESDSGQSALAKS---PNHNLFGIK-GA-YEGNSVSFNTLEADGNQL 392
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696331843 227 KKTKARFRVYGSYVEAVTDYVKLLTQ----NPR-YANV--AAARSPEQGAHALQQAgYATDPQYAQKLVSVIQ 292
Cdd:PRK08581 393 YSINAGFRKYPSTKESLEDYADLIKNgidgNSTiYKPTwkSEAKSYKDATSHLSKT-YATDPNYAKKLNSIIK 464
|
|
| Rod-binding |
pfam10135 |
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ... |
49-95 |
3.16e-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: 57.60 E-value: 3.16e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 696331843 49 KSMRSALPQDGVM--NSDQTRLYTSMYDQQVAQQMS-AKGLGLADMMVEQ 95
Cdd:pfam10135 1 KSMRKTVPKEDGLfdGSEAEDMFRDMLDQQLAKQLAkGGGLGLADMLYRQ 50
|
|
| flgJ |
PRK12708 |
peptidoglycan hydrolase; Reviewed |
25-138 |
5.68e-11 |
|
peptidoglycan hydrolase; Reviewed
Pssm-ID: 139168 [Multi-domain] Cd Length: 134 Bit Score: 59.47 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 25 ARDPQGNLRQVAQQVEGMFVQMMLKSMRSA----LPQDGVMNSDQTRLYTSMYDQQVAQQMSA-KGLGLADMMVEQLSGS 99
Cdd:PRK12708 21 QNLEQGALKLAAQQFEAQFLQTVLKQMRSAsdvmADEDDPFNSKNQGMYRDFYDAELASRLSSqRSMGLAEVMIKQLSSK 100
|
90 100 110
....*....|....*....|....*....|....*....
gi 696331843 100 TSPSEtagtvpmmldnEVLQTLPAQALAQMVRRAMPTPP 138
Cdd:PRK12708 101 LKSAP-----------EVVALESQTLTTTAMQPALIVPP 128
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
160-291 |
5.07e-09 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 57.01 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 160 AQIASQQSgIPHQLIVAQAALESGWGQREIPTAdgkTSYNVFGIKAGSNWDGPVSEiTTTEYEQGVAKKTKARFRVYGSY 239
Cdd:PRK06347 162 SQIAAEND-LYASVMIAQAILESAYGTSELGSA---PNYNLFGIKGAYNGQSYTKQ-TLEDDGKGNYYTITAKFRKYPSY 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 696331843 240 VEAVTDYVKLLTQNPR-----YANV--AAARSPEQGAHALqQAGYATDPQYAQKLVSVI 291
Cdd:PRK06347 237 HQSLEDYAQVIRKGPSwnpnyYSKVwkSNTTSYKDATKAL-TGTYATDTAYATKLNDLI 294
|
|
| LytD |
COG4193 |
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]; |
163-294 |
1.40e-08 |
|
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
Pssm-ID: 443347 [Multi-domain] Cd Length: 423 Bit Score: 55.36 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 163 ASQQSGIPHQLIVAQAALESGWGQREI---PTADGKTSYNVFGIKA-GSNwdgPVSEITTTEYEQGVAKKTKArfrVYGS 238
Cdd:COG4193 281 AAKKYGVNPLYLASHALLETGNGTSKLakgVEVNGKTYYNLFGIGAyDSN---PLENGAKYAYKQGWTSPEKA---IVGG 354
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 696331843 239 YVEAVTDYVKLLT--QNPRYanvAAARSPEQGAHALQqagYATDPQYAQKLVSVIQQM 294
Cdd:COG4193 355 AKFIGSNYINNTGygQNTLY---KMRWNPVNPGTNHQ---YATDPFWAEKIAGHMYRA 406
|
|
| PRK10356 |
PRK10356 |
protein bax; |
169-263 |
2.89e-03 |
|
protein bax;
Pssm-ID: 182404 Cd Length: 274 Bit Score: 38.70 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696331843 169 IPHQLIVAQAALESGWGQREIptadGKTSYNVFGIKAGSNwdgpvseitTTEYEQGvakKTKArFRVYGSYVEAVTDYVK 248
Cdd:PRK10356 149 IPTSMVATMAAAESGWGTSKL----ARNNNNLFGMKCMKG---------RCTNAPG---KVKG-YSQFSSVKESVSAYVT 211
|
90
....*....|....*
gi 696331843 249 LLTQNPRYANVAAAR 263
Cdd:PRK10356 212 NLNTHPAYSSFRKSR 226
|
|
| Bax |
COG2992 |
Uncharacterized FlgJ-related protein [General function prediction only]; |
169-185 |
9.57e-03 |
|
Uncharacterized FlgJ-related protein [General function prediction only];
Pssm-ID: 442231 Cd Length: 253 Bit Score: 36.83 E-value: 9.57e-03
|
| |
