FTSX_ECOLI
ID FTSX_ECOLI Reviewed; 352 AA.
AC P0AC30; P10122; Q2M7C5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cell division protein FtsX;
GN Name=ftsX; Synonyms=ftsS; OrderedLocusNames=b3462, JW3427;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3025556; DOI=10.1007/bf02428043;
RA Gill D.R., Hatfull G.F., Salmond G.P.C.;
RT "A new cell division operon in Escherichia coli.";
RL Mol. Gen. Genet. 205:134-145(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP GENE NAME.
RX PubMed=6394955; DOI=10.1007/bf00330978;
RA Salmond G.P., Plakidou S.;
RT "Genetic analysis of essential genes in the ftsE region of the Escherichia
RT coli genetic map and identification of a new cell division gene, ftsS.";
RL Mol. Gen. Genet. 197:304-308(1984).
RN [6]
RP SUBCELLULAR LOCATION, AND OPERON STRUCTURE.
RX PubMed=3323846; DOI=10.1007/bf00327204;
RA Gill D.R., Salmond G.P.;
RT "The Escherichia coli cell division proteins FtsY, FtsE and FtsX are inner
RT membrane-associated.";
RL Mol. Gen. Genet. 210:504-508(1987).
RN [7]
RP FUNCTION, INTERACTION WITH FTSE, SUBCELLULAR LOCATION, AND OVEREXPRESSION.
RX PubMed=10048040; DOI=10.1046/j.1365-2958.1999.01245.x;
RA de Leeuw E., Graham B., Phillips G.J., ten Hagen-Jongman C.M., Oudega B.,
RA Luirink J.;
RT "Molecular characterization of Escherichia coli FtsE and FtsX.";
RL Mol. Microbiol. 31:983-993(1999).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14729705; DOI=10.1128/jb.186.3.785-793.2004;
RA Schmidt K.L., Peterson N.D., Kustusch R.J., Wissel M.C., Graham B.,
RA Phillips G.J., Weiss D.S.;
RT "A predicted ABC transporter, FtsEX, is needed for cell division in
RT Escherichia coli.";
RL J. Bacteriol. 186:785-793(2004).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=17071757; DOI=10.1128/jb.01347-06;
RA Reddy M.;
RT "Role of FtsEX in cell division of Escherichia coli: viability of ftsEX
RT mutants is dependent on functional SufI or high osmotic strength.";
RL J. Bacteriol. 189:98-108(2007).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular
CC division. Important for assembly or stability of the septal ring.
CC Encoded in an operon consisting of genes ftsY, ftsE and ftsX.
CC {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:14729705}.
CC -!- SUBUNIT: Forms a membrane-associated complex with FtsE.
CC -!- INTERACTION:
CC P0AC30; P37690: envC; NbExp=2; IntAct=EBI-1119111, EBI-15948725;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10048040,
CC ECO:0000269|PubMed:14729705, ECO:0000269|PubMed:3323846}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10048040,
CC ECO:0000269|PubMed:14729705, ECO:0000269|PubMed:3323846}.
CC Note=Localizes to the septal ring at the later stages of cell growth
CC and remains there until division is complete. This localization is
CC dependent on localization of FtsZ, FtsA and ZipA, but not on the
CC downstream division proteins FtsK, FtsQ or FtsI.
CC -!- DISRUPTION PHENOTYPE: Double deletion mutant FtsEX grows well on plates
CC with LB medium with 1% NaCl forming healthy colonies at 30 degrees
CC Celsius, whereas at 37 or 42 degrees Celsius, the colonies are very
CC tiny and sick. In culture medium it exhibits mild elongation of cells
CC at 30 degrees Celsius, and become very extensive at higher
CC temperatures. This double mutant does not grow on LB culture medium
CC without NaCl (LBON) at any temperature, possibly due to excessive
CC lethal filamentation. Supplementation with any of a variety of
CC osmolytes, such as glucose, sucrose, glycerol, or NaCl, completely
CC rescues the growth on LBON medium. Though the growth is completely
CC inhibited on LBON plates, the cultures grown in LBON broth show an
CC initial increase in cell mass before the cessation of growth, and at
CC this stage, the culture is extremely filamentous. The filaments grown
CC in LB at 42 degrees Celsius or in LBON at 30 degrees Celsius are very
CC long and appear to have elongated cells. They are normal and regularly
CC spaced without any significant chromosomal aberrations or partition
CC defects. {ECO:0000269|PubMed:17071757}.
CC -!- MISCELLANEOUS: Overexpression leads to strong inhibition of growth,
CC cell filamentation and eventually cell death.
CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. FtsX
CC subfamily. {ECO:0000305}.
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DR EMBL; X04398; CAA27986.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18437.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76487.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77831.1; -; Genomic_DNA.
DR PIR; S03132; CEECFX.
DR RefSeq; NP_417919.1; NC_000913.3.
DR RefSeq; WP_001042003.1; NZ_STEB01000004.1.
DR PDB; 6TPI; X-ray; 2.10 A; B/C=110-209.
DR PDBsum; 6TPI; -.
DR AlphaFoldDB; P0AC30; -.
DR SMR; P0AC30; -.
DR BioGRID; 4262498; 606.
DR ComplexPortal; CPX-4602; FtsEX ABC cell division complex.
DR DIP; DIP-35993N; -.
DR IntAct; P0AC30; 7.
DR STRING; 511145.b3462; -.
DR ChEMBL; CHEMBL3309011; -.
DR jPOST; P0AC30; -.
DR PaxDb; P0AC30; -.
DR PRIDE; P0AC30; -.
DR EnsemblBacteria; AAC76487; AAC76487; b3462.
DR EnsemblBacteria; BAE77831; BAE77831; BAE77831.
DR GeneID; 66672654; -.
DR GeneID; 947969; -.
DR KEGG; ecj:JW3427; -.
DR KEGG; eco:b3462; -.
DR PATRIC; fig|511145.12.peg.3561; -.
DR EchoBASE; EB0341; -.
DR eggNOG; COG2177; Bacteria.
DR HOGENOM; CLU_073546_0_0_6; -.
DR InParanoid; P0AC30; -.
DR OMA; ETGIMRL; -.
DR PhylomeDB; P0AC30; -.
DR BioCyc; EcoCyc:FTSX-MON; -.
DR PRO; PR:P0AC30; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:0000935; C:division septum; IDA:ComplexPortal.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal.
DR GO; GO:0051301; P:cell division; IMP:EcoliWiki.
DR GO; GO:0000917; P:division septum assembly; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC:ComplexPortal.
DR GO; GO:0009254; P:peptidoglycan turnover; IC:ComplexPortal.
DR GO; GO:0051781; P:positive regulation of cell division; IDA:ComplexPortal.
DR InterPro; IPR004513; ABC_transpt_FtsX.
DR InterPro; IPR040690; FtsX_ECD.
DR PANTHER; PTHR47755; PTHR47755; 1.
DR Pfam; PF18075; FtsX_ECD; 1.
DR PIRSF; PIRSF003097; FtsX; 1.
DR TIGRFAMs; TIGR00439; ftsX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..352
FT /note="Cell division protein FtsX"
FT /id="PRO_0000166792"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..223
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..322
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 19..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:6TPI"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:6TPI"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6TPI"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6TPI"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:6TPI"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:6TPI"
SQ SEQUENCE 352 AA; 38544 MW; C006ED56043739AE CRC64;
MNKRDAINHI RQFGGRLDRF RKSVGGSGDG GRNAPKRAKS SPKPVNRKTN VFNEQVRYAF
HGALQDLKSK PFATFLTVMV IAISLTLPSV CYMVYKNVNQ AATQYYPSPQ ITVYLQKTLD
DDAAAGVVAQ LQAEQGVEKV NYLSREDALG EFRNWSGFGG ALDMLEENPL PAVAVVIPKL
DFQGTESLNT LRDRITQING IDEVRMDDSW FARLAALTGL VGRVSAMIGV LMVAAVFLVI
GNSVRLSIFA RRDSINVQKL IGATDGFILR PFLYGGALLG FSGALLSLIL SEILVLRLSS
AVAEVAQVFG TKFDINGLSF DECLLLLLVC SMIGWVAAWL ATVQHLRHFT PE
