VATA_CHLTR
ID VATA_CHLTR Reviewed; 591 AA.
AC O84310;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=CT_308;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67901.1; -; Genomic_DNA.
DR PIR; B71531; B71531.
DR RefSeq; NP_219813.1; NC_000117.1.
DR RefSeq; WP_009871655.1; NC_000117.1.
DR AlphaFoldDB; O84310; -.
DR SMR; O84310; -.
DR STRING; 813.O172_01650; -.
DR EnsemblBacteria; AAC67901; AAC67901; CT_308.
DR GeneID; 884810; -.
DR KEGG; ctr:CT_308; -.
DR PATRIC; fig|272561.5.peg.329; -.
DR HOGENOM; CLU_008162_1_1_0; -.
DR InParanoid; O84310; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000431; 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; IBA:GO_Central.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
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; Reference proteome; Translocase; Transport.
FT CHAIN 1..591
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144613"
FT BINDING 242..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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