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Conserved domains on  [gi|488223773|ref|WP_002294981|]
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MULTISPECIES: permease-like cell division protein FtsX [Enterococcus]

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, ...
2-293 8.81e-162

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: 451.50  E-value: 8.81e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   2 IRTFFRHLLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELN 81
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIEELEDKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  82 DLDHVKKVEFSSKEQELKKIQNEMGDSWK---LFEGDNNPLYDVYVVSATDPSYTKQVAEEAADLKNVSRSDYGGASSDR 158
Cdd:NF038347  81 KIPGVKSVTFSSKEEELEKLKESLGEEGKlleLLEGDNNPLPDAFIVKVKDPEDVKSVAKIIEKLDGVEKVNYGQGVVEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 159 IFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITF 238
Cdd:NF038347 161 LFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGALLGLLGAIIPILILYF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488223773 239 GYAWFFQLINPSLL-RSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:NF038347 241 GYQYLYNKLNGSLLfSFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
 
Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-293 8.81e-162

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: 451.50  E-value: 8.81e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   2 IRTFFRHLLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELN 81
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIEELEDKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  82 DLDHVKKVEFSSKEQELKKIQNEMGDSWK---LFEGDNNPLYDVYVVSATDPSYTKQVAEEAADLKNVSRSDYGGASSDR 158
Cdd:NF038347  81 KIPGVKSVTFSSKEEELEKLKESLGEEGKlleLLEGDNNPLPDAFIVKVKDPEDVKSVAKIIEKLDGVEKVNYGQGVVEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 159 IFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITF 238
Cdd:NF038347 161 LFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGALLGLLGAIIPILILYF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488223773 239 GYAWFFQLINPSLL-RSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:NF038347 241 GYQYLYNKLNGSLLfSFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
FtsX COG2177
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
4-293 1.84e-92

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


Pssm-ID: 441780 [Multi-domain]  Cd Length: 292  Bit Score: 275.55  E-value: 1.84e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   4 TFFRHLLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELNDL 83
Cdd:COG2177    2 RLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLKDDATEAQIAALEEKLRAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  84 DHVKKVEFSSKEQELKKIQNEMGDSWKLFEGDNNPLYDVYVVSAT--DPSYTKQVAEEAADLKNVSRSDYGGASSDRIFQ 161
Cdd:COG2177   82 PGVASVRYISKEEALEELKEWLGESDLLELLDENPLPASIEVKLKpeDPEDLEALAAALEALPGVAEVDYDREWVERLFA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 162 IAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITFGYA 241
Cdd:COG2177  162 LLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGLLGGLLALLLLALLYL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488223773 242 WFFQLINPSLlrSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:COG2177  242 LLVSALADGL--AFLSLLSLGGLLLLLLLLLLLLGALLGALGSRLAVRRYLR 291
FtsX_actino NF038346
permease-like cell division protein FtsX;
6-293 2.42e-40

permease-like cell division protein FtsX;


Pssm-ID: 468487 [Multi-domain]  Cd Length: 307  Bit Score: 142.26  E-value: 2.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   6 FRHLL-ESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVF------------VDIGTKDEE 72
Cdd:NF038346   1 ARFVLsEVGTGLRRNLTMTIAVILTTAVSLTFLGAGLLLQRQVDKMKGYWYDKVEVSVFlctdvsstdpncAGGAATQEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  73 MKKLEKELNDLD---HVKKVEFSSKEQELKKIQNEMGDSWKLFEG---DNNPlyDVYVVSATDPSYTKQVAEEAAdlknv 146
Cdd:NF038346  81 RDAIRADLESDPlvpLVESVYYESKEEAYERFFKEQFKDSPLADSvtpDDMP--ASFRVKLKDPETKYQVVAEAF----- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 147 srSDYGGASS--------DRIFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFF 218
Cdd:NF038346 154 --SGRPGVESvvdqrellDPLFSVLNGATWAALGLAAVMLVAAVLLIANTIRLSAFSRRRETGIMRLVGASNWYIQLPFI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488223773 219 LEGGWIGLIGAILPILIITFGYAWFFQLINPSLLRSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:NF038346 232 LEGVIAALIGALLAVGGLVAGKYFLVDGWLALSLTFIIAFIGWGDVVLLVAPWLLLVGVLLAAIASWVTLRRYLR 306
FtsX_ECD pfam18075
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
58-148 2.16e-23

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: 91.40  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   58 VDVSVFVDIGTKDEEMKKLEKELNDLDHVKKVEFSSKEQELKKIQNEMGDSWKLFEG--DNNPLYDVYVVSATDPSYTKQ 135
Cdd:pfam18075   1 VEISVFLDDDATEEQIEALEAKLEALPGVKSVTFVSKEEALEEFKEQLGEDPDLLEGltGDNNLPDSFEVKLKDPEQVEA 80
                          90
                  ....*....|...
gi 488223773  136 VAEEAADLKNVSR 148
Cdd:pfam18075  81 IAEQIKGLPGVDE 93
ftsX TIGR00439
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
16-238 3.67e-17

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: 79.90  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   16 LKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELNDLDHVKKVEFSSKE 95
Cdd:TIGR00439  24 LRQQPFGTLLTLIVIAVSLTLPLVMYLGIKNGQSALTQLYPSPQITVYLEKALAQSDADTVVSLLTRDKGVENINYISRE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   96 QELKKIQNEMGDSWKLFEGDNNPLYDVYVVSatdPSYTKQVAEEAADLKN-------VSRSDYGGASSDRIFQIAGAVRT 168
Cdd:TIGR00439 104 DGLAEFQSWSGFGNLLSMLDGNPLPAVFIVT---PDPAFTPAEMQAILRDnitkipgVEEVRMDTEWVQTLYALNELIRK 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488223773  169 WgLVAAALLLFVAMFL-ISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITF 238
Cdd:TIGR00439 181 V-LWFLSVLMGMAVFLvIGNSIRLQILSRRESIEVTKLLGATDSFILRPFLYQGMWQSIFGALVSLILSGW 250
ftsX PRK11026
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
9-234 5.04e-15

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: 73.86  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   9 LLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELNDLDHVKK 88
Cdd:PRK11026  17 WRGALADLKRKPLATLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTVYLDKTLDDDAANAVVEQLKAEDGVEK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  89 VEFSSKEQELKKIQNEMGDSWKLFEGDNNPLYDVYVVSatdPSYTKQVAEEAADLKnvsrsdyggassDRIFQIAGA--V 166
Cdd:PRK11026  97 VNYLSREEALGEFRNWSGFGGALDMLEENPLPAVAIII---PKLDFQSSEKLNTLR------------DRLAQIKGVdeV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 167 R------------TW--GLVAA--ALLLFVAMFL-ISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGA 229
Cdd:PRK11026 162 RmddswfarlaalTGlvGRVAAmiGVLMVAAVFLvIGNSVRLSIFSRRDTINVMKLIGATDGFILRPFLYGGALLGFSGA 241

                 ....*
gi 488223773 230 ILPIL 234
Cdd:PRK11026 242 LLSLI 246
 
Name Accession Description Interval E-value
FtsX_Gpos NF038347
permease-like cell division protein FtsX; The FtsEX complex resembles an ABC transporter, ...
2-293 8.81e-162

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: 451.50  E-value: 8.81e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   2 IRTFFRHLLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELN 81
Cdd:NF038347   1 IRTFFRHLREAFKSLKRNGWMTFASVSAVTVTLLLLGVFLLLILNVNKLASDVESDVEIRVYLDDDATDEQIEELEDKIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  82 DLDHVKKVEFSSKEQELKKIQNEMGDSWK---LFEGDNNPLYDVYVVSATDPSYTKQVAEEAADLKNVSRSDYGGASSDR 158
Cdd:NF038347  81 KIPGVKSVTFSSKEEELEKLKESLGEEGKlleLLEGDNNPLPDAFIVKVKDPEDVKSVAKIIEKLDGVEKVNYGQGVVEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 159 IFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITF 238
Cdd:NF038347 161 LFKITKTVRNVGLVLIVLLAFTAMFLISNTIRITIFARRREIEIMKLVGATNWFIRWPFFLEGALLGLLGAIIPILILYF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488223773 239 GYAWFFQLINPSLL-RSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:NF038347 241 GYQYLYNKLNGSLLfSFLISLLPPNPFLLQISGLLLLIGILIGALGSVISVRKFLK 296
FtsX COG2177
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
4-293 1.84e-92

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


Pssm-ID: 441780 [Multi-domain]  Cd Length: 292  Bit Score: 275.55  E-value: 1.84e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   4 TFFRHLLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELNDL 83
Cdd:COG2177    2 RLLYALREALRGLRRNPLMTLASILVIALALLLLGLFLLLLLNANQLASQLEDEVEISVYLKDDATEAQIAALEEKLRAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  84 DHVKKVEFSSKEQELKKIQNEMGDSWKLFEGDNNPLYDVYVVSAT--DPSYTKQVAEEAADLKNVSRSDYGGASSDRIFQ 161
Cdd:COG2177   82 PGVASVRYISKEEALEELKEWLGESDLLELLDENPLPASIEVKLKpeDPEDLEALAAALEALPGVAEVDYDREWVERLFA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 162 IAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITFGYA 241
Cdd:COG2177  162 LLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGLLGGLLALLLLALLYL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488223773 242 WFFQLINPSLlrSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:COG2177  242 LLVSALADGL--AFLSLLSLGGLLLLLLLLLLLLGALLGALGSRLAVRRYLR 291
FtsX_actino NF038346
permease-like cell division protein FtsX;
6-293 2.42e-40

permease-like cell division protein FtsX;


Pssm-ID: 468487 [Multi-domain]  Cd Length: 307  Bit Score: 142.26  E-value: 2.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   6 FRHLL-ESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVF------------VDIGTKDEE 72
Cdd:NF038346   1 ARFVLsEVGTGLRRNLTMTIAVILTTAVSLTFLGAGLLLQRQVDKMKGYWYDKVEVSVFlctdvsstdpncAGGAATQEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  73 MKKLEKELNDLD---HVKKVEFSSKEQELKKIQNEMGDSWKLFEG---DNNPlyDVYVVSATDPSYTKQVAEEAAdlknv 146
Cdd:NF038346  81 RDAIRADLESDPlvpLVESVYYESKEEAYERFFKEQFKDSPLADSvtpDDMP--ASFRVKLKDPETKYQVVAEAF----- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 147 srSDYGGASS--------DRIFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFF 218
Cdd:NF038346 154 --SGRPGVESvvdqrellDPLFSVLNGATWAALGLAAVMLVAAVLLIANTIRLSAFSRRRETGIMRLVGASNWYIQLPFI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488223773 219 LEGGWIGLIGAILPILIITFGYAWFFQLINPSLLRSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:NF038346 232 LEGVIAALIGALLAVGGLVAGKYFLVDGWLALSLTFIIAFIGWGDVVLLVAPWLLLVGVLLAAIASWVTLRRYLR 306
FtsX_ECD pfam18075
FtsX extracellular domain; This is the extracellular domain (ECD) found in FtsX enzyme, a ...
58-148 2.16e-23

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: 91.40  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   58 VDVSVFVDIGTKDEEMKKLEKELNDLDHVKKVEFSSKEQELKKIQNEMGDSWKLFEG--DNNPLYDVYVVSATDPSYTKQ 135
Cdd:pfam18075   1 VEISVFLDDDATEEQIEALEAKLEALPGVKSVTFVSKEEALEEFKEQLGEDPDLLEGltGDNNLPDSFEVKLKDPEQVEA 80
                          90
                  ....*....|...
gi 488223773  136 VAEEAADLKNVSR 148
Cdd:pfam18075  81 IAEQIKGLPGVDE 93
LolE COG4591
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ...
120-293 7.66e-18

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: 81.51  E-value: 7.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 120 YDVYVVSATDPSYTKQVAEEAADLKNVSRSDYGGASSDRIFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQRE 199
Cdd:COG4591  103 VSGILVKLKDGADAEAVAAALEAALPGLEVKTWRELNAALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTRE 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 200 IQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILpILIITFGYAWFFQLINPSLLRSHYSLihPQNIVWKINLLMVGIGVII 279
Cdd:COG4591  183 IGILKALGASRRQIRRIFLLEGLLLGLIGGLL-GLLLGLLLALLLNALLGILLPFIFAL--PVSLSPSDVLLALLLALLI 259
                        170
                 ....*....|....
gi 488223773 280 GSLGSIISMRRFLK 293
Cdd:COG4591  260 SLLASLYPARRAAR 273
ftsX TIGR00439
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
16-238 3.67e-17

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: 79.90  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   16 LKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELNDLDHVKKVEFSSKE 95
Cdd:TIGR00439  24 LRQQPFGTLLTLIVIAVSLTLPLVMYLGIKNGQSALTQLYPSPQITVYLEKALAQSDADTVVSLLTRDKGVENINYISRE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   96 QELKKIQNEMGDSWKLFEGDNNPLYDVYVVSatdPSYTKQVAEEAADLKN-------VSRSDYGGASSDRIFQIAGAVRT 168
Cdd:TIGR00439 104 DGLAEFQSWSGFGNLLSMLDGNPLPAVFIVT---PDPAFTPAEMQAILRDnitkipgVEEVRMDTEWVQTLYALNELIRK 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488223773  169 WgLVAAALLLFVAMFL-ISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIITF 238
Cdd:TIGR00439 181 V-LWFLSVLMGMAVFLvIGNSIRLQILSRRESIEVTKLLGATDSFILRPFLYQGMWQSIFGALVSLILSGW 250
ftsX PRK11026
putative protein insertion permease FtsX; FtsX is an integral membrane protein encoded in the ...
9-234 5.04e-15

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: 73.86  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773   9 LLESIKSLKRNGWMTVASVSAVTITLTLVGVFMAVIMNATKLAQDIEGNVDVSVFVDIGTKDEEMKKLEKELNDLDHVKK 88
Cdd:PRK11026  17 WRGALADLKRKPLATLLTVMVIAISLTLPSVCYLVWKNVNQAATQWYPSPQLTVYLDKTLDDDAANAVVEQLKAEDGVEK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  89 VEFSSKEQELKKIQNEMGDSWKLFEGDNNPLYDVYVVSatdPSYTKQVAEEAADLKnvsrsdyggassDRIFQIAGA--V 166
Cdd:PRK11026  97 VNYLSREEALGEFRNWSGFGGALDMLEENPLPAVAIII---PKLDFQSSEKLNTLR------------DRLAQIKGVdeV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 167 R------------TW--GLVAA--ALLLFVAMFL-ISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGA 229
Cdd:PRK11026 162 RmddswfarlaalTGlvGRVAAmiGVLMVAAVFLvIGNSVRLSIFSRRDTINVMKLIGATDGFILRPFLYGGALLGFSGA 241

                 ....*
gi 488223773 230 ILPIL 234
Cdd:PRK11026 242 LLSLI 246
SalY COG0577
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
157-290 5.02e-12

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


Pssm-ID: 440342 [Multi-domain]  Cd Length: 339  Bit Score: 65.30  E-value: 5.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 157 DRIFQIAGAVRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILII 236
Cdd:COG0577  204 AALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFLTEALLLALLGGLLGLLLA 283
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488223773 237 TFGYAWFFQLINPSLLrshyslihpqnIVWKINLLMVGIGVIIGSLGSIISMRR 290
Cdd:COG0577  284 LLLLRLLAALLGLPVS-----------LDPWVLLLALALSLLVGLLAGLYPARR 326
FtsX pfam02687
FtsX-like permease family; This is a family of predicted permeases and hypothetical ...
171-293 5.53e-10

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: 56.10  E-value: 5.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773  171 LVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILpILIITFGYAWFFqlinpS 250
Cdd:pfam02687   1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVI-GLLLGLLLAKLI-----A 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 488223773  251 LLRSHYSLIHPQNIVWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:pfam02687  75 ILLYSSGISLPILVPPLSILIALLLALLIALLASLLPALRIRK 117
YbbP COG3127
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
161-293 6.82e-10

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: 59.81  E-value: 6.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 161 QIAGAVRtwglVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILiITFGY 240
Cdd:COG3127  702 QVSLAVE----FLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLAAL-LAELA 776
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488223773 241 AWFFQLinpSLLRSHYSLIhpqnivWKINLLMVGIGVIIGSLGSIISMRRFLK 293
Cdd:COG3127  777 GWALAR---FVFDLPFSPP------WWLWLAGLLGGALLVLLAGLLGARRVLR 820
YbbP COG3127
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ...
171-286 7.21e-09

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: 56.35  E-value: 7.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 171 LVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILIitfgyAWFFQLINPS 250
Cdd:COG3127  257 LLVALLALLLAGVAVANAARRYVARRLDTIALLRCLGASRRQIFRIYLLQLLLLGLLGSLLGLLL-----GALLQALLAA 331
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488223773 251 LLRshySLIhPQNIVWKINLLMVGIGVIIGSLGSII 286
Cdd:COG3127  332 LLA---DLL-PVPLEPALSPLPLLLGLLVGLLVLLL 363
PRK11146 PRK11146
lipoprotein-releasing ABC transporter permease subunit LolE;
166-235 6.11e-04

lipoprotein-releasing ABC transporter permease subunit LolE;


Pssm-ID: 236860 [Multi-domain]  Cd Length: 412  Bit Score: 41.04  E-value: 6.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223773 166 VRTWGLVAAALLLFVAMFLISNTIRITILSRQREIQIMRLVGAKNGYIRWPFFLEGGWIGLIGAILPILI 235
Cdd:PRK11146 266 IRTIMYLAMVLVIGVACFNIVSTLVMAVKDKSGDIAILRTLGAKDGLIRAIFVWYGLLAGLKGSLIGVVI 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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