ATPZ_ECOL6
ID ATPZ_ECOL6 Reviewed; 126 AA.
AC P0ABC1; P03808; P76747; Q47248;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=ATP synthase protein I;
GN Name=atpI; OrderedLocusNames=c4667;
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: A possible function for this protein is to guide the assembly
CC of the membrane sector of the ATPase enzyme complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial AtpI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN83099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN83099.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000116695.1; NC_004431.1.
DR AlphaFoldDB; P0ABC1; -.
DR STRING; 199310.c4667; -.
DR EnsemblBacteria; AAN83099; AAN83099; c4667.
DR GeneID; 66672357; -.
DR KEGG; ecc:c4667; -.
DR eggNOG; COG3312; Bacteria.
DR HOGENOM; CLU_121415_2_0_6; -.
DR OMA; YMYMQVE; -.
DR Proteomes; UP000001410; Chromosome.
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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR005598; ATP_synth_I.
DR Pfam; PF03899; ATP-synt_I; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..126
FT /note="ATP synthase protein I"
FT /id="PRO_0000071707"
FT TOPO_DOM 2..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..37
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 126 AA; 13632 MW; 308FC1C16059C5A6 CRC64;
MSVSLVSRNV ARKLLLVQLL VVIASGLLFS LKDPFWGVSA ISGGLAVFLP NVLFMIFAWR
HQAHTPAKGR VAWTFAFGEA FKVLAMLVLL VVALAVLKAV FLPLIVTWVL VLVVQILAPA
VINNKG