ID VATA_CHLTB Reviewed; 591 AA.
AC B0BBT9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=CTLon_0556;
OS Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCH-1/proctitis;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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; AM884177; CAP06954.1; -; Genomic_DNA.
DR RefSeq; WP_009873713.1; NC_010280.2.
DR AlphaFoldDB; B0BBT9; -.
DR SMR; B0BBT9; -.
DR KEGG; ctl:CTLon_0556; -.
DR HOGENOM; CLU_008162_1_1_0; -.
DR Proteomes; UP001154401; 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 CDD; cd01426; ATP-synt_F1_V1_A1_AB_FliI_N; 1.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.30.30.650; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 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; P-loop containing nucleoside triphosphate hydrolases; 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_1000115635"
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; 65495 MW; 7DB64F8A33901723 CRC64;
MVATSKQTTQ GYVVEAYGNL LRVHVDGHVR QGEVAYVSVD NTWLKAEIIE VVGDEVKIQV
FEETQGISRG ALVTFSGHLL EAELGPGLLQ GIFDGLQNRL EILADTSLFL RRGEYVNAIC
RETVWAYTQK ASVGSVLSRG DVLGTVKEGR FDHKIMVPFS CFEEVTITWV ISSGNYTVDT
VVAKGRTSTG EELEFTMVQK WPIKQAFLEG EKVPSHEIMD VGLRVLDTQI PVLKGGTFCT
PGPFGAGKTV LQHHLSKYAA VDIVVLCACG ERAGEVVEIL QEFPHLKDPH 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 A
//
