ID   VATA_CHLPN              Reviewed;         591 AA.
AC   Q9Z993;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 142.
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=CPn_0088, CP_0686, CpB0088;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AE001363; AAD18241.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38495.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98298.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98021.1; -; Genomic_DNA.
DR   PIR; B72121; B72121.
DR   PIR; H86501; H86501.
DR   RefSeq; NP_224296.1; NC_000922.1.
DR   RefSeq; WP_010882738.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z993; -.
DR   SMR; Q9Z993; -.
DR   STRING; 115711.CP_0686; -.
DR   EnsemblBacteria; AAD18241; AAD18241; CPn_0088.
DR   EnsemblBacteria; AAF38495; AAF38495; CP_0686.
DR   GeneID; 45050133; -.
DR   KEGG; cpa:CP_0686; -.
DR   KEGG; cpj:atpA; -.
DR   KEGG; cpn:CPn_0088; -.
DR   KEGG; cpt:CpB0088; -.
DR   PATRIC; fig|115713.3.peg.101; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_1_1_0; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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_0000144612"
FT   BINDING         242..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   591 AA;  65360 MW;  2CCEBFCCD99A4938 CRC64;
     MVTVSEQTAQ GHVIEAYGNL LRVRFDGYVR QGEVAYVNVD NTWLKAEVIE VADQEVKVQV
     FEDTQGACRG ALVTFSGHLL EAELGPGLLQ GIFDGLQNRL EVLAEDSSFL QRGKHVNAIS
     DHNLWNYTPV ASVGDTLRRG DLLGTVPEGR FTHKIMVPFS CFQEVTLTWV ISEGTYNAHT
     VVAKARDAQG KECAFTMVQR WPIKQAFIEG EKIPAHKIMD VGLRILDTQI PVLKGGTFCT
     PGPFGAGKTV LQHHLSKYAA VDIVILCACG ERAGEVVEVL QEFPHLIDPH TGKSLMHRTC
     IICNTSSMPV AARESSIYLG VTIAEYYRQM GLDILLLADS TSRWAQALRE ISGRLEEIPG
     EEAFPAYLSS RIAAFYERGG AITTKDGSEG SLTICGAVSP AGGNFEEPVT QSTLAVVGAF
     CGLSKARADA RRYPSIDPLI SWSKYLNQVG QILEEKVSGW GGAVKKAAQF LEKGSEIGKR
     MEVVGEEGVS MEDMEIYLKA ELYDFCYLQQ NAFDPVDCYC PFERQIELFS LISRIFDAKF
     VFDSPDDARS FFLELQSKIK TLNGLKFLSE EYHESKEVIV RLLEKTMVQM A