ID   ATP61_BRUA4             Reviewed;         249 AA.
AC   A6WW77;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   02-SEP-2026, entry version 99.
DE   RecName: Full=ATP synthase subunit a 1 {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a 1 {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 1 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB1 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   OrderedLocusNames=Oant_0500;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 /
RC   NBRC 15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
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DR   EMBL; CP000758; ABS13231.1; -; Genomic_DNA.
DR   RefSeq; WP_010658321.1; NC_009667.1.
DR   AlphaFoldDB; A6WW77; -.
DR   SMR; A6WW77; -.
DR   STRING; 439375.Oant_0500; -.
DR   GeneID; 61316669; -.
DR   KEGG; oan:Oant_0500; -.
DR   PATRIC; fig|439375.7.peg.534; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_0_2_5; -.
DR   PhylomeDB; A6WW77; -.
DR   Proteomes; UP000002301; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   CDD; cd00310; ATP-synt_Fo_a_6; 1.
DR   FunFam; 1.20.120.220:FF:000003; ATP synthase subunit a; 1.
DR   Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   NCBIfam; TIGR01131; ATP_synt_6_or_A; 1.
DR   NCBIfam; NF004482; PRK05815.2-4; 1.
DR   PANTHER; PTHR11410; ATP SYNTHASE SUBUNIT A; 1.
DR   PANTHER; PTHR11410:SF0; ATP SYNTHASE SUBUNIT A; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..249
FT                   /note="ATP synthase subunit a 1"
FT                   /id="PRO_0000362359"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   249 AA;  26805 MW;  B44A92A17676489C CRC64;
     MANDPIHQFQ VSRWIPIDVG GVDLSFTNVS AFMVATVVVA SGFLYLTSSG RGLIPTRLQS
     VSEMAYEFVA TSLRDSAGSK GMKFFPFVFS LFMFVLVANF LGLFPYFYTV TSQIIVTFAL
     AVLVIGTVIV YGFFKHGLGF LKLFVPSGVP GIIVPLVVAI EIISFLSRPI SLSVRLFANM
     LAGHITLKVF AGFVVSLAAL GPIGIGGAVL PLIMTVAITA LEFLVAFLQA YVFTVLTCMY
     INDAVHPGH
//