ID   ATP6_BACP2              Reviewed;         244 AA.
AC   A8FIB8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BPUM_3332;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(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 membrane {ECO:0000255|HAMAP-Rule:MF_01393};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000813; ABV63985.1; -; Genomic_DNA.
DR   RefSeq; WP_012011551.1; NZ_VEIS01000002.1.
DR   AlphaFoldDB; A8FIB8; -.
DR   SMR; A8FIB8; -.
DR   STRING; 315750.BPUM_3332; -.
DR   EnsemblBacteria; ABV63985; ABV63985; BPUM_3332.
DR   KEGG; bpu:BPUM_3332; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_2_3_9; -.
DR   OMA; FTHAVRL; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000001355; 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; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR42823; PTHR42823; 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 membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..244
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_1000145259"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        171..191
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        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   244 AA;  26963 MW;  0A5FC7C1A99608D8 CRC64;
     MGHSSKTTEF LGLTFNLSNV LMITIASIIV LLIAVLTTRV LSIRPTKAQN FMEWIVDFVR
     NIIGSSMDMK TGAPFLALGV TLLMYIFVSN MLGLPFSISV DHNLWWKSPT ADPAITMTLA
     VMVMGLTHYY GVKAKGVKEY TKDYFRPIPL LVPLKIIEEF ANTLTLGLRL YGNIFAGEIL
     LGLLAGLATN FYSQNIALGI IGTLGAIVPM IVWQAFSLFV GTIQAFIFTM LTMVYISHKV
     SDEH