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Conserved domains on  [gi|499202189|ref|WP_010899729|]
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permease-like cell division protein FtsX [Halalkalibacterium halodurans]

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, ...
3-297 4.40e-151

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: 424.53  E-value: 4.40e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   3 FRTLSRHVREGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQ 82
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIEELEDKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  83 TIPNIESVTYVSRDEGLDQLIGSLDEEtAPVFESLRE-ENPLNDKFVVRATNPQLTEQIADQIEAMNHVDYVRFGREVVN 161
Cdd:NF038347  81 KIPGVKSVTFSSKEEELEKLKESLGEE-GKLLELLEGdNNPLPDAFIVKVKDPEDVKSVAKIIEKLDGVEKVNYGQGVVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 162 RLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILW 241
Cdd:NF038347 160 KLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGALLGLLGAIIPILILY 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499202189 242 GGYYYVYNNFGGQVQ-NFLFSLTPVTPSILQVAVVLVAVGAFIGMWGSVMSVRKFLK 297
Cdd:NF038347 240 FGYQYLYNKLNGSLLfSFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
 
Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
3-297 4.40e-151

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: 424.53  E-value: 4.40e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   3 FRTLSRHVREGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQ 82
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIEELEDKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  83 TIPNIESVTYVSRDEGLDQLIGSLDEEtAPVFESLRE-ENPLNDKFVVRATNPQLTEQIADQIEAMNHVDYVRFGREVVN 161
Cdd:NF038347  81 KIPGVKSVTFSSKEEELEKLKESLGEE-GKLLELLEGdNNPLPDAFIVKVKDPEDVKSVAKIIEKLDGVEKVNYGQGVVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 162 RLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILW 241
Cdd:NF038347 160 KLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGALLGLLGAIIPILILY 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499202189 242 GGYYYVYNNFGGQVQ-NFLFSLTPVTPSILQVAVVLVAVGAFIGMWGSVMSVRKFLK 297
Cdd:NF038347 240 FGYQYLYNKLNGSLLfSFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
FtsX COG2177
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
5-298 9.81e-96

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


Pssm-ID: 441780 [Multi-domain]  Cd Length: 292  Bit Score: 284.03  E-value: 9.81e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   5 TLSRHVREGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQTI 84
Cdd:COG2177    2 RLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLKDDATEAQIAALEEKLRAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  85 PNIESVTYVSRDEGLDQLIGSLDEETApvFESLrEENPLNDKFVVRAT--NPQLTEQIADQIEAMNHVDYVRFGREVVNR 162
Cdd:COG2177   82 PGVASVRYISKEEALEELKEWLGESDL--LELL-DENPLPASIEVKLKpeDPEDLEALAAALEALPGVAEVDYDREWVER 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 163 LFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILWG 242
Cdd:COG2177  159 LFALLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGLLGGLLALLLLAL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499202189 243 GYYYVYNNFGGQVQnfLFSLTPVTPSILQVAVVLVAVGAFIGMWGSVMSVRKFLKV 298
Cdd:COG2177  239 LYLLLVSALADGLA--FLSLLSLGGLLLLLLLLLLLLGALLGALGSRLAVRRYLRV 292
FtsX_actino NF038346
permease-like cell division protein FtsX;
11-266 3.36e-43

permease-like cell division protein FtsX;


Pssm-ID: 468487 [Multi-domain]  Cd Length: 307  Bit Score: 149.96  E-value: 3.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  11 REGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYieLTADKT--------------QQEA 76
Cdd:NF038346   6 SEVGTGLRRNLTMTIAVILTTAVSLTFLGAGLLLQRQVDKMKGYWYDKVEVSVF--LCTDVSstdpncaggaatqeQRDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  77 LEAEIQT---IPNIESVTYVSRDEGLDQLIgSLDEETAPVFESLREEnPLNDKFVVRATNPQLTEQ-IADQIEAMNHVDY 152
Cdd:NF038346  84 IRADLESdplVPLVESVYYESKEEAYERFF-KEQFKDSPLADSVTPD-DMPASFRVKLKDPETKYQvVAEAFSGRPGVES 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 153 VRFGREVVNRLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIG 232
Cdd:NF038346 162 VVDQRELLDPLFSVLNGATWAALGLAAVMLVAAVLLIANTIRLSAFSRRRETGIMRLVGASNWYIQLPFILEGVIAALIG 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 499202189 233 ALIPIAILWGGYYYVYNNFGGQVqnFLFSLTPVT 266
Cdd:NF038346 242 ALLAVGGLVAGKYFLVDGWLALS--LTFIIAFIG 273
ftsX TIGR00439
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
24-235 2.33e-30

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: 116.11  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   24 TFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQTIPNIESVTYVSRDEGLDQLI 103
Cdd:TIGR00439  31 TLLTLIVIAVSLTLPLVMYLGIKNGQSALTQLYPSPQITVYLEKALAQSDADTVVSLLTRDKGVENINYISREDGLAEFQ 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  104 G-SLDEETApvfeSLREENPLNDKFVVR---ATNP-QLTEQIADQIEAMNHVDYVRFGREVVNRLFTITNFVRTGGLVLI 178
Cdd:TIGR00439 111 SwSGFGNLL----SMLDGNPLPAVFIVTpdpAFTPaEMQAILRDNITKIPGVEEVRMDTEWVQTLYALNELIRKVLWFLS 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499202189  179 IGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALI 235
Cdd:TIGR00439 187 VLMGMAVFLVIGNSIRLQILSRRESIEVTKLLGATDSFILRPFLYQGMWQSIFGALV 243
FtsX_ECD pfam18075
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
59-153 2.39e-28

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: 104.50  E-value: 2.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   59 VEINVYIELTADKTQQEALEAEIQTIPNIESVTYVSRDEGLDQLIGSLDEETApVFESLREENPLNDKFVVRATNPQLTE 138
Cdd:pfam18075   1 VEISVFLDDDATEEQIEALEAKLEALPGVKSVTFVSKEEALEEFKEQLGEDPD-LLEGLTGDNNLPDSFEVKLKDPEQVE 79
                          90
                  ....*....|....*
gi 499202189  139 QIADQIEAMNHVDYV 153
Cdd:pfam18075  80 AIAEQIKGLPGVDEV 94
ftsX PRK11026
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
24-237 8.15e-27

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: 106.60  E-value: 8.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  24 TFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQTIPNIESVTYVSRDEGLDQLI 103
Cdd:PRK11026  31 TLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTVYLDKTLDDDAANAVVEQLKAEDGVEKVNYLSREEALGEFR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 104 ------GSLDeetapvfesLREENPLNDKFVVRAT----NPQLTEQIADQIEAMNHVDYVRFGREVVNRLFTITNFVrtG 173
Cdd:PRK11026 111 nwsgfgGALD---------MLEENPLPAVAIIIPKldfqSSEKLNTLRDRLAQIKGVDEVRMDDSWFARLAALTGLV--G 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499202189 174 GLVLIIG-MMLTAMFL-ISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPI 237
Cdd:PRK11026 180 RVAAMIGvLMVAAVFLvIGNSVRLSIFSRRDTINVMKLIGATDGFILRPFLYGGALLGFSGALLSL 245
 
Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
3-297 4.40e-151

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: 424.53  E-value: 4.40e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   3 FRTLSRHVREGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQ 82
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIEELEDKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  83 TIPNIESVTYVSRDEGLDQLIGSLDEEtAPVFESLRE-ENPLNDKFVVRATNPQLTEQIADQIEAMNHVDYVRFGREVVN 161
Cdd:NF038347  81 KIPGVKSVTFSSKEEELEKLKESLGEE-GKLLELLEGdNNPLPDAFIVKVKDPEDVKSVAKIIEKLDGVEKVNYGQGVVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 162 RLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILW 241
Cdd:NF038347 160 KLFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGALLGLLGAIIPILILY 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499202189 242 GGYYYVYNNFGGQVQ-NFLFSLTPVTPSILQVAVVLVAVGAFIGMWGSVMSVRKFLK 297
Cdd:NF038347 240 FGYQYLYNKLNGSLLfSFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
FtsX COG2177
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
5-298 9.81e-96

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


Pssm-ID: 441780 [Multi-domain]  Cd Length: 292  Bit Score: 284.03  E-value: 9.81e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   5 TLSRHVREGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQTI 84
Cdd:COG2177    2 RLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLKDDATEAQIAALEEKLRAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  85 PNIESVTYVSRDEGLDQLIGSLDEETApvFESLrEENPLNDKFVVRAT--NPQLTEQIADQIEAMNHVDYVRFGREVVNR 162
Cdd:COG2177   82 PGVASVRYISKEEALEELKEWLGESDL--LELL-DENPLPASIEVKLKpeDPEDLEALAAALEALPGVAEVDYDREWVER 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 163 LFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILWG 242
Cdd:COG2177  159 LFALLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGLLGGLLALLLLAL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499202189 243 GYYYVYNNFGGQVQnfLFSLTPVTPSILQVAVVLVAVGAFIGMWGSVMSVRKFLKV 298
Cdd:COG2177  239 LYLLLVSALADGLA--FLSLLSLGGLLLLLLLLLLLLGALLGALGSRLAVRRYLRV 292
FtsX_actino NF038346
permease-like cell division protein FtsX;
11-266 3.36e-43

permease-like cell division protein FtsX;


Pssm-ID: 468487 [Multi-domain]  Cd Length: 307  Bit Score: 149.96  E-value: 3.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  11 REGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYieLTADKT--------------QQEA 76
Cdd:NF038346   6 SEVGTGLRRNLTMTIAVILTTAVSLTFLGAGLLLQRQVDKMKGYWYDKVEVSVF--LCTDVSstdpncaggaatqeQRDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  77 LEAEIQT---IPNIESVTYVSRDEGLDQLIgSLDEETAPVFESLREEnPLNDKFVVRATNPQLTEQ-IADQIEAMNHVDY 152
Cdd:NF038346  84 IRADLESdplVPLVESVYYESKEEAYERFF-KEQFKDSPLADSVTPD-DMPASFRVKLKDPETKYQvVAEAFSGRPGVES 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 153 VRFGREVVNRLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIG 232
Cdd:NF038346 162 VVDQRELLDPLFSVLNGATWAALGLAAVMLVAAVLLIANTIRLSAFSRRRETGIMRLVGASNWYIQLPFILEGVIAALIG 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 499202189 233 ALIPIAILWGGYYYVYNNFGGQVqnFLFSLTPVT 266
Cdd:NF038346 242 ALLAVGGLVAGKYFLVDGWLALS--LTFIIAFIG 273
ftsX TIGR00439
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
24-235 2.33e-30

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: 116.11  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   24 TFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQTIPNIESVTYVSRDEGLDQLI 103
Cdd:TIGR00439  31 TLLTLIVIAVSLTLPLVMYLGIKNGQSALTQLYPSPQITVYLEKALAQSDADTVVSLLTRDKGVENINYISREDGLAEFQ 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  104 G-SLDEETApvfeSLREENPLNDKFVVR---ATNP-QLTEQIADQIEAMNHVDYVRFGREVVNRLFTITNFVRTGGLVLI 178
Cdd:TIGR00439 111 SwSGFGNLL----SMLDGNPLPAVFIVTpdpAFTPaEMQAILRDNITKIPGVEEVRMDTEWVQTLYALNELIRKVLWFLS 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499202189  179 IGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALI 235
Cdd:TIGR00439 187 VLMGMAVFLVIGNSIRLQILSRRESIEVTKLLGATDSFILRPFLYQGMWQSIFGALV 243
FtsX_ECD pfam18075
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
59-153 2.39e-28

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: 104.50  E-value: 2.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   59 VEINVYIELTADKTQQEALEAEIQTIPNIESVTYVSRDEGLDQLIGSLDEETApVFESLREENPLNDKFVVRATNPQLTE 138
Cdd:pfam18075   1 VEISVFLDDDATEEQIEALEAKLEALPGVKSVTFVSKEEALEEFKEQLGEDPD-LLEGLTGDNNLPDSFEVKLKDPEQVE 79
                          90
                  ....*....|....*
gi 499202189  139 QIADQIEAMNHVDYV 153
Cdd:pfam18075  80 AIAEQIKGLPGVDEV 94
ftsX PRK11026
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
24-237 8.15e-27

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: 106.60  E-value: 8.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  24 TFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYIELTADKTQQEALEAEIQTIPNIESVTYVSRDEGLDQLI 103
Cdd:PRK11026  31 TLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTVYLDKTLDDDAANAVVEQLKAEDGVEKVNYLSREEALGEFR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 104 ------GSLDeetapvfesLREENPLNDKFVVRAT----NPQLTEQIADQIEAMNHVDYVRFGREVVNRLFTITNFVrtG 173
Cdd:PRK11026 111 nwsgfgGALD---------MLEENPLPAVAIIIPKldfqSSEKLNTLRDRLAQIKGVDEVRMDDSWFARLAALTGLV--G 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499202189 174 GLVLIIG-MMLTAMFL-ISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPI 237
Cdd:PRK11026 180 RVAAMIGvLMVAAVFLvIGNSVRLSIFSRRDTINVMKLIGATDGFILRPFLYGGALLGFSGALLSL 245
LolE COG4591
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ...
127-262 1.80e-16

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: 77.65  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 127 FVVRATNPQLTEQIADQIEAMNHVDYVRFGREVVNRLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKLTIFARKREIQI 206
Cdd:COG4591  106 ILVKLKDGADAEAVAAALEAALPGLEVKTWRELNAALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGI 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499202189 207 MKLVGATNGFIRWPFFIEGILLGVIGALIPIAILWGGYYYVyNNFGGQVQNFLFSL 262
Cdd:COG4591  186 LKALGASRRQIRRIFLLEGLLLGLIGGLLGLLLGLLLALLL-NALLGILLPFIFAL 240
SalY COG0577
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
8-266 1.02e-08

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


Pssm-ID: 440342 [Multi-domain]  Cd Length: 339  Bit Score: 55.67  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189   8 RHVREGTKNLGRNGWMTFASISAVAVMLFVVGAFILMIMNMNQVATTVEDDVEINVYI-----ELTADKTQQEALEAEIQ 82
Cdd:COG0577    1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTvsrtpGGSRATLSYEDLREALR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  83 TIPNIESVTYVSRDEGLDQLIGSLDEETAPVF----------------------------------ESLRE-----ENPL 123
Cdd:COG0577   81 ALPGVESVAPSSSGSATVRYGGGEPPSVRVLGvdpdyfrvlgipllagrfftaaddlgappvvvigEALARrlfggEDPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 124 NDkfVVRATNPQLT------EQIADQIEAMNHVD--YVRFGREVVNRLFTITNFVRTGGLVLIIGMMLTAMFLISNTIKL 195
Cdd:COG0577  161 GK--TIRLNGRPFTvvgvveAELRALLRRRDPGDdfEVQTLDEILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLA 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499202189 196 TIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILWGGYYYVynnfgGQVQNFLFSLTPVT 266
Cdd:COG0577  239 SVTERTREIGIRKALGASRRDILRQFLTEALLLALLGGLLGLLLALLLLRLL-----AALLGLPVSLDPWV 304
YbbP COG3127
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
157-247 1.67e-08

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: 55.58  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 157 REVVNRLFTITNFVrtGGLVLIIGMMLtamflISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIP 236
Cdd:COG3127  697 RDILDQVSLAVEFL--AGFALLAGLLV-----LAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLA 769
                         90
                 ....*....|....*
gi 499202189 237 I----AILWGGYYYV 247
Cdd:COG3127  770 AllaeLAGWALARFV 784
FtsX pfam02687
FtsX-like permease family; This is a family of predicted permeases and hypothetical ...
175-265 4.70e-08

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: 50.71  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189  175 LVLIIGMMLTAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAILWGGYYYVYNNFGGQ 254
Cdd:pfam02687   1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLIAILLYSS 80
                          90
                  ....*....|.
gi 499202189  255 VQNFLFSLTPV 265
Cdd:pfam02687  81 GISLPILVPPL 91
YbbP COG3127
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
135-242 8.41e-05

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: 44.02  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499202189 135 QLTEQIADQIEAMNHVDYVRFGREVVNRLFT-ITNFVrtgGLVLIIGMMLtAMFLISNTIKLTIFARKREIQIMKLVGAT 213
Cdd:COG3127  220 ALRAWLEPALPAGQRVRTVEDARPELGRALDrAEQFL---LLVALLALLL-AGVAVANAARRYVARRLDTIALLRCLGAS 295
                         90       100
                 ....*....|....*....|....*....
gi 499202189 214 NGFIRWPFFIEGILLGVIGALIPIAILWG 242
Cdd:COG3127  296 RRQIFRIYLLQLLLLGLLGSLLGLLLGAL 324
PRK11146 PRK11146
lipoprotein-releasing ABC transporter permease subunit LolE;
175-239 1.08e-04

lipoprotein-releasing ABC transporter permease subunit LolE;


Pssm-ID: 236860 [Multi-domain]  Cd Length: 412  Bit Score: 43.35  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499202189 175 LVLIIGMmltAMFLISNTIKLTIFARKREIQIMKLVGATNGFIRWPFFIEGILLGVIGALIPIAI 239
Cdd:PRK11146 274 MVLVIGV---ACFNIVSTLVMAVKDKSGDIAILRTLGAKDGLIRAIFVWYGLLAGLKGSLIGVVI 335
 
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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