ID   ATP6_BART1              Reviewed;         252 AA.
AC   A9IQH9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=BT_0622;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK01060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM260525; CAK01060.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_038474497.1; NC_010161.1.
DR   AlphaFoldDB; A9IQH9; -.
DR   SMR; A9IQH9; -.
DR   STRING; 382640.BT_0622; -.
DR   EnsemblBacteria; CAK01060; CAK01060; BT_0622.
DR   KEGG; btr:BT_0622; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_0_2_5; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000001592; 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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.220; -; 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   PANTHER; PTHR11410; PTHR11410; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..252
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000362242"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   252 AA;  27502 MW;  36F0C7A2EE96DC05 CRC64;
     MTAHAPDPIH QFEVSRLIKI SIGNMDLSFT NVSLFTVVTV VITAAFLFIS SSSRGLVPTR
     MQSLSEMAYE FVASTLRESS GVQGMQFFPL VFSLFTFILV ANFIGLFPYF YTVTSQIMIT
     FSLAMVVILT VIGYGFYKHG ISFLKLFVPS GVPVVVLPLV TMIEIISFLS RPISLSLRLF
     ANMLAGHITL KVFAGFIVSM IGVGIVGVGG AVLPLIMTVA ITALEFLVAF LQAYVFTVLT
     CMYLNDAIHP GH