ID   ATP6_PSEAE              Reviewed;         289 AA.
AC   Q9HT14;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=PA5560;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG08945.1; -; Genomic_DNA.
DR   PIR; A82953; A82953.
DR   RefSeq; NP_254247.1; NC_002516.2.
DR   RefSeq; WP_003100237.1; NZ_QZGE01000012.1.
DR   AlphaFoldDB; Q9HT14; -.
DR   SMR; Q9HT14; -.
DR   STRING; 287.DR97_2939; -.
DR   PaxDb; Q9HT14; -.
DR   PRIDE; Q9HT14; -.
DR   DNASU; 880089; -.
DR   EnsemblBacteria; AAG08945; AAG08945; PA5560.
DR   GeneID; 880089; -.
DR   KEGG; pae:PA5560; -.
DR   PATRIC; fig|208964.12.peg.5826; -.
DR   PseudoCAP; PA5560; -.
DR   HOGENOM; CLU_041018_1_0_6; -.
DR   InParanoid; Q9HT14; -.
DR   OMA; FTHAVRL; -.
DR   PhylomeDB; Q9HT14; -.
DR   BioCyc; PAER208964:G1FZ6-5687-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IBA:GO_Central.
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   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..289
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000287745"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        160..180
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        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   289 AA;  31921 MW;  49CCB34633991395 CRC64;
     MAAETASGYI QHHLQNLTFG RLPNGDWGFA HTAEQAKEMG FWAFHVDTLG WSVLLGVVFL
     FIFRLAAKKA TSGQPGGLQN FVEVMVEFVD TSVKDTFHGR NPLIAPLALT VFVWIFLLNL
     IDLVPVDYLP MLAAKITGDE HLFFRAVATT DPNATLGLSI SVFALIVFYS IKVKGIGGFL
     GELTLHPFSS KNIVVQILLI PVNFLLEFVT LIAKPVSLAL RLFGNMYAGE LIFILIAVMF
     GSGMFLLSAL GVALNWAWAV FHILIITLQA FIFMMLTIVY LSMAHEDNH