FTSX_ECOL6
ID FTSX_ECOL6 Reviewed; 352 AA.
AC P0AC31; P10122;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cell division protein FtsX;
GN Name=ftsX; OrderedLocusNames=c4255;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a membrane-associated complex with FtsE. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Localizes to the septal ring at
CC the later stages of cell growth and remains there until division is
CC complete. This localization is dependent on localization of FtsZ, FtsA
CC and ZipA, but not on the downstream division proteins FtsK, FtsQ or
CC FtsI (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. FtsX
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82691.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82691.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001042003.1; NC_004431.1.
DR AlphaFoldDB; P0AC31; -.
DR SMR; P0AC31; -.
DR STRING; 199310.c4255; -.
DR TCDB; 3.A.1.140.1; the atp-binding cassette (abc) superfamily.
DR PRIDE; P0AC31; -.
DR EnsemblBacteria; AAN82691; AAN82691; c4255.
DR GeneID; 66672654; -.
DR KEGG; ecc:c4255; -.
DR eggNOG; COG2177; Bacteria.
DR HOGENOM; CLU_073546_0_0_6; -.
DR OMA; ETGIMRL; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Cell division protein FtsX"
FT /id="PRO_0000166793"
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"
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