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Conserved domains on  [gi|489155986|ref|WP_003065667|]
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MULTISPECIES: permease-like cell division protein FtsX [Streptococcus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-308 7.85e-161

permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages.


:

Pssm-ID: 468488 [Multi-domain]  Cd Length: 296  Bit Score: 449.96  E-value: 7.85e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   2 IRNFFRHLWESIKSLKRNVWMTVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDVDSTDSSETttnevge 81
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIE------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  82 tvtndsyhQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWT---LFDGDSNPLQDVYIVEADSPSDVKKVANKITKI 158
Cdd:NF038347  74 --------ELEDKIEKIPGVKSVTFSSKEEELEKLKESLGEEGKlleLLEGDNNPLPDAFIVKVKDPEDVKSVAKIIEKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 159 EGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAW 238
Cdd:NF038347 146 DGVEKVNYGQGVVEKLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGAL 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489155986 239 VGLLGAIVPSIIIYFAYKTVYSSVNPQFEV-QGLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLK 308
Cdd:NF038347 226 LGLLGAIIPILILYFGYQYLYNKLNGSLLFsFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
 
Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-308 7.85e-161

permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages.


Pssm-ID: 468488 [Multi-domain]  Cd Length: 296  Bit Score: 449.96  E-value: 7.85e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   2 IRNFFRHLWESIKSLKRNVWMTVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDVDSTDSSETttnevge 81
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIE------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  82 tvtndsyhQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWT---LFDGDSNPLQDVYIVEADSPSDVKKVANKITKI 158
Cdd:NF038347  74 --------ELEDKIEKIPGVKSVTFSSKEEELEKLKESLGEEGKlleLLEGDNNPLPDAFIVKVKDPEDVKSVAKIIEKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 159 EGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAW 238
Cdd:NF038347 146 DGVEKVNYGQGVVEKLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGAL 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489155986 239 VGLLGAIVPSIIIYFAYKTVYSSVNPQFEV-QGLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLK 308
Cdd:NF038347 226 LGLLGAIIPILILYFGYQYLYNKLNGSLLFsFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
FtsX COG2177
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
4-308 5.96e-96

Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441780 [Multi-domain]  Cd Length: 292  Bit Score: 285.18  E-value: 5.96e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   4 NFFRHLWESIKSLKRNVWMTVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDvdstdssetttnevgETV 83
Cdd:COG2177    2 RLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLK---------------DDA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  84 TNDSYHQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWTLFDGDSNPLQDVYIVE--ADSPSDVKKVANKITKIEGV 161
Cdd:COG2177   67 TEAQIAALEEKLRALPGVASVRYISKEEALEELKEWLGESDLLELLDENPLPASIEVKlkPEDPEDLEALAAALEALPGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 162 ESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGL 241
Cdd:COG2177  147 AEVDYDREWVERLFALLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGL 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489155986 242 LGAIVPSIIIYFAYKTVYSSVNPQFEVqgLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLK 308
Cdd:COG2177  227 LGGLLALLLLALLYLLLVSALADGLAF--LSLLSLGGLLLLLLLLLLLLGALLGALGSRLAVRRYLR 291
FtsX_actino NF038346
permease-like cell division protein FtsX;
11-309 1.29e-44

permease-like cell division protein FtsX;


Pssm-ID: 468487 [Multi-domain]  Cd Length: 307  Bit Score: 153.81  E-value: 1.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  11 ESIKSLKRNVWMTVASVSSVTITLTLVGvfAAVLLN--VERIATGIENNIQINVYLdvdSTDSSETTTNEVGETVTNDSY 88
Cdd:NF038346   7 EVGTGLRRNLTMTIAVILTTAVSLTFLG--AGLLLQrqVDKMKGYWYDKVEVSVFL---CTDVSSTDPNCAGGAATQEQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  89 HQVYDQISK---VSGVESVTYSSKDEQLEKLQEAYGDDWTLFDG---DSnpLQDVYIVE-ADSPSDVKKVANKITKIEGV 161
Cdd:NF038346  82 DAIRADLESdplVPLVESVYYESKEEAYERFFKEQFKDSPLADSvtpDD--MPASFRVKlKDPETKYQVVAEAFSGRPGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 162 ESVdyggsnSDQ------LFSIAKFIR--TWGFAGtvLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFF 233
Cdd:NF038346 160 ESV------VDQrelldpLFSVLNGATwaALGLAA--VMLVAAVLLIANTIRLSAFSRRRETGIMRLVGASNWYIQLPFI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489155986 234 FEGAWVGLLGAIVPSIIIYFAYKTVYSSVNPQFEVQGLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLKI 309
Cdd:NF038346 232 LEGVIAALIGALLAVGGLVAGKYFLVDGWLALSLTFIIAFIGWGDVVLLVAPWLLLVGVLLAAIASWVTLRRYLRV 307
ftsX TIGR00439
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
2-307 1.99e-31

putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 129531 [Multi-domain]  Cd Length: 309  Bit Score: 119.19  E-value: 1.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986    2 IRNFFRHLWESIKSLKRNVWMTVASVSsvtITLTLVGVFAAVLLNVERIATGIENNIQINVYLDVDSTDSSETTtnevge 81
Cdd:TIGR00439  13 VEYARSALKQDLRQQPFGTLLTLIVIA---VSLTLPLVMYLGIKNGQSALTQLYPSPQITVYLEKALAQSDADT------ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   82 tvtndsyhqVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWTLFDGDSNPLQDVYIVEADSPSDVKKVAN----KITK 157
Cdd:TIGR00439  84 ---------VVSLLTRDKGVENINYISREDGLAEFQSWSGFGNLLSMLDGNPLPAVFIVTPDPAFTPAEMQAilrdNITK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  158 IEGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGA 237
Cdd:TIGR00439 155 IPGVEEVRMDTEWVQTLYALNELIRKVLWFLSVLMGMAVFLVIGNSIRLQILSRRESIEVTKLLGATDSFILRPFLYQGM 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489155986  238 WVGLLGAIVPSIIIYFAYKTVYSSVNPQFEVQGLSL----YPVDTFLPLviggmFLVGIIIGALGSVISMRRYL 307
Cdd:TIGR00439 235 WQSIFGALVSLILSGWLLSAVRSAVDAVFKPFGLNFgwngLYVGELGLL-----LGFCIALGVVGAWLATTQHL 303
ftsX PRK11026
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
1-308 7.57e-26

putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 182910 [Multi-domain]  Cd Length: 309  Bit Score: 104.29  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   1 MIRNFFRHLWESIKSLKRNVWM--------TVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDvdstdss 72
Cdd:PRK11026   1 HIRQFTNGFNEQVRYAWRGALAdlkrkplaTLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTVYLD------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  73 etttnevgETVTNDSYHQVYDQISKVSGVESVTYSSKDEQLEKLQeaygdDWTLFDG-----DSNPLQDVYIV----EAD 143
Cdd:PRK11026  74 --------KTLDDDAANAVVEQLKAEDGVEKVNYLSREEALGEFR-----NWSGFGGaldmlEENPLPAVAIIipklDFQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 144 SPSDVKKVANKITKIEGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIfVAIFL-ISNTIRMTIMSRQRDIEIMRLVG 222
Cdd:PRK11026 141 SSEKLNTLRDRLAQIKGVDEVRMDDSWFARLAALTGLVGRVAAMIGVLMV-AAVFLvIGNSVRLSIFSRRDTINVMKLIG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 223 AKNSYIRGPFFFEGAWVGLLGAIVPSI-----IIYF--AYKTVYSSVNPQFEVQGLSLypvDTFLPLviggmFLVGIIIG 295
Cdd:PRK11026 220 ATDGFILRPFLYGGALLGFSGALLSLIlseilVWRLssAVTYVADVFGTKFDLNGLSF---DECLLL-----LLVCSMIG 291
                        330
                 ....*....|...
gi 489155986 296 ALGSVISMRRYLK 308
Cdd:PRK11026 292 WVAAWLATVQHLR 304
FtsX_ECD pfam18075
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
58-164 7.86e-22

FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a homolog of the transmembrane PG-hydrolase regulator. The FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme ileading to PG hydrolysis in Mycobacterium tuberculosis. Structural analysis of FtsX ECD reveals fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes showed reduction in RipC binding in vitro and inhibition of FtsX function in Mycobacterium smegmatis.


Pssm-ID: 465634 [Multi-domain]  Cd Length: 94  Bit Score: 87.55  E-value: 7.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   58 IQINVYLDVDSTDSSETttnevgetvtndsyhQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWTLFDG--DSNPLQ 135
Cdd:pfam18075   1 VEISVFLDDDATEEQIE---------------ALEAKLEALPGVKSVTFVSKEEALEEFKEQLGEDPDLLEGltGDNNLP 65
                          90       100
                  ....*....|....*....|....*....
gi 489155986  136 DVYIVEADSPSDVKKVANKITKIEGVESV 164
Cdd:pfam18075  66 DSFEVKLKDPEQVEAIAEQIKGLPGVDEV 94
 
Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-308 7.85e-161

permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages.


Pssm-ID: 468488 [Multi-domain]  Cd Length: 296  Bit Score: 449.96  E-value: 7.85e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   2 IRNFFRHLWESIKSLKRNVWMTVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDVDSTDSSETttnevge 81
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIE------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  82 tvtndsyhQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWT---LFDGDSNPLQDVYIVEADSPSDVKKVANKITKI 158
Cdd:NF038347  74 --------ELEDKIEKIPGVKSVTFSSKEEELEKLKESLGEEGKlleLLEGDNNPLPDAFIVKVKDPEDVKSVAKIIEKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 159 EGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAW 238
Cdd:NF038347 146 DGVEKVNYGQGVVEKLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGAL 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489155986 239 VGLLGAIVPSIIIYFAYKTVYSSVNPQFEV-QGLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLK 308
Cdd:NF038347 226 LGLLGAIIPILILYFGYQYLYNKLNGSLLFsFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
FtsX COG2177
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
4-308 5.96e-96

Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441780 [Multi-domain]  Cd Length: 292  Bit Score: 285.18  E-value: 5.96e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   4 NFFRHLWESIKSLKRNVWMTVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDvdstdssetttnevgETV 83
Cdd:COG2177    2 RLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLK---------------DDA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  84 TNDSYHQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWTLFDGDSNPLQDVYIVE--ADSPSDVKKVANKITKIEGV 161
Cdd:COG2177   67 TEAQIAALEEKLRALPGVASVRYISKEEALEELKEWLGESDLLELLDENPLPASIEVKlkPEDPEDLEALAAALEALPGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 162 ESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGL 241
Cdd:COG2177  147 AEVDYDREWVERLFALLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGL 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489155986 242 LGAIVPSIIIYFAYKTVYSSVNPQFEVqgLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLK 308
Cdd:COG2177  227 LGGLLALLLLALLYLLLVSALADGLAF--LSLLSLGGLLLLLLLLLLLLGALLGALGSRLAVRRYLR 291
FtsX_actino NF038346
permease-like cell division protein FtsX;
11-309 1.29e-44

permease-like cell division protein FtsX;


Pssm-ID: 468487 [Multi-domain]  Cd Length: 307  Bit Score: 153.81  E-value: 1.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  11 ESIKSLKRNVWMTVASVSSVTITLTLVGvfAAVLLN--VERIATGIENNIQINVYLdvdSTDSSETTTNEVGETVTNDSY 88
Cdd:NF038346   7 EVGTGLRRNLTMTIAVILTTAVSLTFLG--AGLLLQrqVDKMKGYWYDKVEVSVFL---CTDVSSTDPNCAGGAATQEQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  89 HQVYDQISK---VSGVESVTYSSKDEQLEKLQEAYGDDWTLFDG---DSnpLQDVYIVE-ADSPSDVKKVANKITKIEGV 161
Cdd:NF038346  82 DAIRADLESdplVPLVESVYYESKEEAYERFFKEQFKDSPLADSvtpDD--MPASFRVKlKDPETKYQVVAEAFSGRPGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 162 ESVdyggsnSDQ------LFSIAKFIR--TWGFAGtvLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFF 233
Cdd:NF038346 160 ESV------VDQrelldpLFSVLNGATwaALGLAA--VMLVAAVLLIANTIRLSAFSRRRETGIMRLVGASNWYIQLPFI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489155986 234 FEGAWVGLLGAIVPSIIIYFAYKTVYSSVNPQFEVQGLSLYPVDTFLPLVIGGMFLVGIIIGALGSVISMRRYLKI 309
Cdd:NF038346 232 LEGVIAALIGALLAVGGLVAGKYFLVDGWLALSLTFIIAFIGWGDVVLLVAPWLLLVGVLLAAIASWVTLRRYLRV 307
ftsX TIGR00439
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
2-307 1.99e-31

putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 129531 [Multi-domain]  Cd Length: 309  Bit Score: 119.19  E-value: 1.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986    2 IRNFFRHLWESIKSLKRNVWMTVASVSsvtITLTLVGVFAAVLLNVERIATGIENNIQINVYLDVDSTDSSETTtnevge 81
Cdd:TIGR00439  13 VEYARSALKQDLRQQPFGTLLTLIVIA---VSLTLPLVMYLGIKNGQSALTQLYPSPQITVYLEKALAQSDADT------ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   82 tvtndsyhqVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWTLFDGDSNPLQDVYIVEADSPSDVKKVAN----KITK 157
Cdd:TIGR00439  84 ---------VVSLLTRDKGVENINYISREDGLAEFQSWSGFGNLLSMLDGNPLPAVFIVTPDPAFTPAEMQAilrdNITK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  158 IEGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGA 237
Cdd:TIGR00439 155 IPGVEEVRMDTEWVQTLYALNELIRKVLWFLSVLMGMAVFLVIGNSIRLQILSRRESIEVTKLLGATDSFILRPFLYQGM 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489155986  238 WVGLLGAIVPSIIIYFAYKTVYSSVNPQFEVQGLSL----YPVDTFLPLviggmFLVGIIIGALGSVISMRRYL 307
Cdd:TIGR00439 235 WQSIFGALVSLILSGWLLSAVRSAVDAVFKPFGLNFgwngLYVGELGLL-----LGFCIALGVVGAWLATTQHL 303
ftsX PRK11026
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
1-308 7.57e-26

putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. It belongs to a family of predicted permeases and may play a role in the insertion of proteins required for potassium transport, cell division, and other activities. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX. [Cellular processes, Cell division, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 182910 [Multi-domain]  Cd Length: 309  Bit Score: 104.29  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   1 MIRNFFRHLWESIKSLKRNVWM--------TVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYLDvdstdss 72
Cdd:PRK11026   1 HIRQFTNGFNEQVRYAWRGALAdlkrkplaTLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTVYLD------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  73 etttnevgETVTNDSYHQVYDQISKVSGVESVTYSSKDEQLEKLQeaygdDWTLFDG-----DSNPLQDVYIV----EAD 143
Cdd:PRK11026  74 --------KTLDDDAANAVVEQLKAEDGVEKVNYLSREEALGEFR-----NWSGFGGaldmlEENPLPAVAIIipklDFQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 144 SPSDVKKVANKITKIEGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIfVAIFL-ISNTIRMTIMSRQRDIEIMRLVG 222
Cdd:PRK11026 141 SSEKLNTLRDRLAQIKGVDEVRMDDSWFARLAALTGLVGRVAAMIGVLMV-AAVFLvIGNSVRLSIFSRRDTINVMKLIG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 223 AKNSYIRGPFFFEGAWVGLLGAIVPSI-----IIYF--AYKTVYSSVNPQFEVQGLSLypvDTFLPLviggmFLVGIIIG 295
Cdd:PRK11026 220 ATDGFILRPFLYGGALLGFSGALLSLIlseilVWRLssAVTYVADVFGTKFDLNGLSF---DECLLL-----LLVCSMIG 291
                        330
                 ....*....|...
gi 489155986 296 ALGSVISMRRYLK 308
Cdd:PRK11026 292 WVAAWLATVQHLR 304
FtsX_ECD pfam18075
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
58-164 7.86e-22

FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a homolog of the transmembrane PG-hydrolase regulator. The FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme ileading to PG hydrolysis in Mycobacterium tuberculosis. Structural analysis of FtsX ECD reveals fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes showed reduction in RipC binding in vitro and inhibition of FtsX function in Mycobacterium smegmatis.


Pssm-ID: 465634 [Multi-domain]  Cd Length: 94  Bit Score: 87.55  E-value: 7.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   58 IQINVYLDVDSTDSSETttnevgetvtndsyhQVYDQISKVSGVESVTYSSKDEQLEKLQEAYGDDWTLFDG--DSNPLQ 135
Cdd:pfam18075   1 VEISVFLDDDATEEQIE---------------ALEAKLEALPGVKSVTFVSKEEALEEFKEQLGEDPDLLEGltGDNNLP 65
                          90       100
                  ....*....|....*....|....*....
gi 489155986  136 DVYIVEADSPSDVKKVANKITKIEGVESV 164
Cdd:pfam18075  66 DSFEVKLKDPEQVEAIAEQIKGLPGVDEV 94
LolE COG4591
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ...
79-305 2.49e-17

ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443648 [Multi-domain]  Cd Length: 283  Bit Score: 80.35  E-value: 2.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  79 VGETVTNDSYHQVYDQIS-KVSGVESVTYSSKDEQ-----LEKLQEAYGDDwtlfdgdsnPLQDVYIVEADSPSDVKKVA 152
Cdd:COG4591   50 VGDTITLISPDGSPKTRRfTVVGIFESGGYELDGSlvyvpLETAQELLGLG---------DQVSGILVKLKDGADAEAVA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 153 NKITKIEGVESVDYGGSNSDQLFSIAKFIRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPF 232
Cdd:COG4591  121 AALEAALPGLEVKTWRELNAALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGILKALGASRRQIRRIF 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489155986 233 FFEGAWVGLLGAIVPSIIIYFAykTVYSSVNPQFEVQGLSLYPVdTFLPLVIGGMFLVGIIIGALGSVISMRR 305
Cdd:COG4591  201 LLEGLLLGLIGGLLGLLLGLLL--ALLLNALLGILLPFIFALPV-SLSPSDVLLALLLALLISLLASLYPARR 270
FtsX pfam02687
FtsX-like permease family; This is a family of predicted permeases and hypothetical ...
190-309 9.17e-11

FtsX-like permease family; This is a family of predicted permeases and hypothetical transmembrane proteins. Swiss:P57382 has been shown to transport lipids targeted to the outer membrane across the inner membrane. Both Swiss:P57382 and Swiss:O54500 have been shown to require ATP. This region contains three transmembrane helices.


Pssm-ID: 460652 [Multi-domain]  Cd Length: 120  Bit Score: 58.42  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  190 VLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGLLGAIVPSIIIYFAYKtvYSSVNPQFEVQ 269
Cdd:pfam02687   5 LLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAK--LIAILLYSSGI 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489155986  270 GLSLYpvdtFLPLVIGGMFLVGIIIGALGSVISMRRYLKI 309
Cdd:pfam02687  83 SLPIL----VPPLSILIALLLALLIALLASLLPALRIRKI 118
SalY COG0577
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
7-305 2.29e-09

ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];


Pssm-ID: 440342 [Multi-domain]  Cd Length: 339  Bit Score: 57.60  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986   7 RHLWESIKSLKRNVWMTVASVSSVTITLTLVGVFAAVLLNVERIATGIENNIQINVYldvdstdsseTTTNEVGETVTND 86
Cdd:COG0577    1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLL----------TVSRTPGGSRATL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986  87 SYHQVYDQISKVSGVESVTYSSKDE-----------------------QLEKLQEAYGDDWTLFDGDSNPlqDVYIV--- 140
Cdd:COG0577   71 SYEDLREALRALPGVESVAPSSSGSatvrygggeppsvrvlgvdpdyfRVLGIPLLAGRFFTAADDLGAP--PVVVIgea 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 141 -------EADSPSDVKKVANKITKIEGV-------------ESVDYGGSNSDQLfsIAKFIRTWGFAGTVLLIFVAIFL- 199
Cdd:COG0577  149 larrlfgGEDPVGKTIRLNGRPFTVVGVveaelrallrrrdPGDDFEVQTLDEI--LAALYGVLRTLTLLLGAIAGLALl 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 200 -----ISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGLLGAIVPSIIIYFAYKTvyssvnpqfeVQGLSLY 274
Cdd:COG0577  227 vacigIMNLMLASVTERTREIGIRKALGASRRDILRQFLTEALLLALLGGLLGLLLALLLLRL----------LAALLGL 296
                        330       340       350
                 ....*....|....*....|....*....|.
gi 489155986 275 PVdTFLPLVIGGMFLVGIIIGALGSVISMRR 305
Cdd:COG0577  297 PV-SLDPWVLLLALALSLLVGLLAGLYPARR 326
PRK11146 PRK11146
lipoprotein-releasing ABC transporter permease subunit LolE;
181-250 5.01e-08

lipoprotein-releasing ABC transporter permease subunit LolE;


Pssm-ID: 236860 [Multi-domain]  Cd Length: 412  Bit Score: 53.76  E-value: 5.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 181 IRTWGFAGTVLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGLLGAIVPSII 250
Cdd:PRK11146 266 IRTIMYLAMVLVIGVACFNIVSTLVMAVKDKSGDIAILRTLGAKDGLIRAIFVWYGLLAGLKGSLIGVVI 335
YbbP COG3127
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
182-309 8.43e-07

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442361 [Multi-domain]  Cd Length: 830  Bit Score: 50.18  E-value: 8.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 182 RTWGFAGTVLL------IFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGLLGAIVPSIIIYFAY 255
Cdd:COG3127  247 RALDRAEQFLLlvallaLLLAGVAVANAARRYVARRLDTIALLRCLGASRRQIFRIYLLQLLLLGLLGSLLGLLLGALLQ 326
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489155986 256 KTVYSSVNPQFevqGLSLYPVDTFLPLVIGgmFLVGIIIGALGSVISMRRYLKI 309
Cdd:COG3127  327 ALLAALLADLL---PVPLEPALSPLPLLLG--LLVGLLVLLLFALPPLLRLRRV 375
YbbP COG3127
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
190-308 1.95e-06

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442361 [Multi-domain]  Cd Length: 830  Bit Score: 49.03  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489155986 190 VLLIFVAIFLISNTIRMTIMSRQRDIEIMRLVGAKNSYIRGPFFFEGAWVGLLGAIVPSIIIYFAYKTVYSSVnpqFEvq 269
Cdd:COG3127  712 GFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLAALLAELAGWALARFV---FD-- 786
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489155986 270 gLSLypvdTFLPLVIGGMFLVGIIIGALGSVISMRRYLK 308
Cdd:COG3127  787 -LPF----SPPWWLWLAGLLGGALLVLLAGLLGARRVLR 820
 
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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