ID   VATA_CHLTA              Reviewed;         591 AA.
AC   Q3KM54;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=CTA_0330;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The V-type alpha chain is a catalytic subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
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DR   EMBL; CP000051; AAX50568.1; -; Genomic_DNA.
DR   RefSeq; WP_009871655.1; NC_007429.1.
DR   AlphaFoldDB; Q3KM54; -.
DR   SMR; Q3KM54; -.
DR   EnsemblBacteria; AAX50568; AAX50568; CTA_0330.
DR   KEGG; cta:CTA_0330; -.
DR   HOGENOM; CLU_008162_1_1_0; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000002532; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; PTHR43607; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..591
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_1000059335"
FT   BINDING         242..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   591 AA;  65497 MW;  3780967B6914785F CRC64;
     MVATSKQTTQ GYVVEAYGNL LRVHVDGHVR QGEVAYVSVD DTWLKAEIIE VVGDEVKIQV
     FEETQGISRG ALVTFSGHLL EAELGPGLLQ GIFDGLQNRL EILADTSLFL RRGEYVNAIC
     RETVWAYTQK ASVGSVLSRG DVLGTVKEGR FDHKIMVPFS CFEEVTITWV ISSGNYTVDT
     VVAKGRTSTG EELEFTMVQK WPIKQAFLEG EKVPSHEIMD VGLRVLDTQI PVLKGGTFCT
     PGPFGAGKTV LQHHLSKYAA VDIVVLCACG ERAGEVVEIL QEFPHLTDPH TGQSLMHRTC
     IICNTSSMPV AARESSIYLG ITIAEYYRQM GLHILLLADS TSRWAQALRE ISGRLEEIPG
     EEAFPAYLAS RIAAFYERGG AVKMKDGSEG SLTICGAVSP AGGNFEEPVT QATLSVVGAF
     CGLSKARADA RRYPSIDPMI SWSKYLDSVA EILEKKVPGW GESVKQASRF LEEGAEIGKR
     IEVVGEEGIS MEDMEIFLKS ELYDFCYLQQ NAFDAEDCYC PFDRQIELFS LMNHIFNSRF
     CFDCPDNARS FFLELQSKIK TLNGQKFLSE EYQKGLEVIY KLLESKMVQT V