ID   VATA_CHLMU              Reviewed;         591 AA.
AC   Q9PK85;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=V-type ATP synthase alpha chain;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase subunit A;
GN   Name=atpA; OrderedLocusNames=TC_0582;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE002160; AAF39416.1; -; Genomic_DNA.
DR   PIR; E81687; E81687.
DR   RefSeq; WP_010230899.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PK85; -.
DR   SMR; Q9PK85; -.
DR   STRING; 243161.TC_0582; -.
DR   EnsemblBacteria; AAF39416; AAF39416; TC_0582.
DR   GeneID; 1245941; -.
DR   KEGG; cmu:TC_0582; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_1_1_0; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000000800; 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_0000144611"
FT   BINDING         242..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   591 AA;  65302 MW;  7F8432BAB0741B14 CRC64;
     MVATSKQTTQ GYVVEAYGNL LRVHFDGHVR QGEVAYVSVD DTWLKAEIIE VVGDEVKVQV
     FEETQGISRG ALVTFSGHLL EAELGPGLLQ GIFDGLQNRL EVLADTSLFL KRGEYVNAIC
     RETVWAYTQK ASVGDVLSRG DVLGTVKEGR FDHKIMVPFS CFEEVTITWV ISSGDYTVDT
     VIAKGRTASG AELEFTMVQK WPIKQAFLEG EKVPSHEIMD VGLRVLDTQI PVLKGGTFCT
     PGPFGAGKTV LQHHLSKYAA VDIVVLCACG ERAGEVVEIL QEFPHLTDPH TGQSLMHRTC
     IICNTSSMPV AARESSIYLG ITIAEYYRQM GLHVLLLADS TSRWAQALRE ISGRLEEIPG
     EEAFPAYLAS RIAAFYERGG AVKMKDGSEG SLTICGAVSP AGGNFEEPVT QATLSVVGAF
     CGLSKARADA RRYPSIDPMI SWSKYLDSVA EILEKKVPGW GDSVKKASRF LEEGAEIGKR
     IEVVGEEGIS MEDIEIFLKS ELYDFCYLQQ NAFDAEDCYC PFDRQIELFS LMSHIFSSRF
     CFDCPDNARS FFLELQSKIK TLNGQKFLSE DYQKGLEVIY KLLESKMVQT A