ID   ATP62_METCA             Reviewed;         228 AA.
AC   Q603U8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=ATP synthase subunit a 2 {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a 2 {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 2 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB2 {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=MCA2699;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU91248.1; -; Genomic_DNA.
DR   RefSeq; WP_010961910.1; NC_002977.6.
DR   AlphaFoldDB; Q603U8; -.
DR   SMR; Q603U8; -.
DR   STRING; 243233.MCA2699; -.
DR   EnsemblBacteria; AAU91248; AAU91248; MCA2699.
DR   KEGG; mca:MCA2699; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_2_5_6; -.
DR   OMA; ITIVYYH; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000006821; 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 inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="ATP synthase subunit a 2"
FT                   /id="PRO_0000362348"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   228 AA;  24710 MW;  D2F678A787316D32 CRC64;
     MEQIDFFARV LGHLGPVTVS DSLLTSVLVA GLLSAASAVL TRRRTALPDR VQVVLEGIVS
     ACENAVRDVI PTAYREVTPF IMSLWLFLAT ANLISLVPGF DSPTRDLSVT SALAVLVFFS
     VHWFGIRQQG LSAYLKHYLT PNPVLLPFHL IGEITRTLAL AIRLFGNMMS MELIGLLLLI
     IGGLFVPVPV LLLHVVEGLV QAYIFGILAL VYIAGGIQSG PQQENHSP