VATA_CLOPE
ID VATA_CLOPE Reviewed; 591 AA.
AC Q8XJW5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=CPE1638;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81344.1; -; Genomic_DNA.
DR RefSeq; WP_003449648.1; NC_003366.1.
DR AlphaFoldDB; Q8XJW5; -.
DR SMR; Q8XJW5; -.
DR STRING; 195102.gene:10490902; -.
DR EnsemblBacteria; BAB81344; BAB81344; BAB81344.
DR GeneID; 29571009; -.
DR KEGG; cpe:CPE1638; -.
DR HOGENOM; CLU_008162_3_1_9; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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; 2.40.30.20; -; 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; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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; SSF50615; SSF50615; 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_1000059338"
FT BINDING 232..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 591 AA; 64872 MW; E11939AEC5964E1E CRC64;
MKTGKIIKVS GPLVVAEGMD EANVYDVVKV GEKGLIGEII EMRGDKASIQ VYEETSGIGP
GDPVITTGEP LSVELGPGLI ESMFDGIQRP LDAFMKAANS AFLSKGVEVK SLNREKKWPF
VPTAKVGDKV SAGDVIGTVQ ETAVVLHRIM VPFGVEGTIK EIKAGDFNVE EVIAVVETEK
GDKNLTLMQK WPVRKGRPYA RKLNPVEPMT TGQRVIDTFF PVAKGGAAAV PGPFGAGKTV
VQHQVAKWGD TEIVVYVGCG ERGNEMTDVL NEFPELKDPK TGESLMKRTV LIANTSNMPV
AAREASIYTG ITIAEYFRDM GYSVSIMADS TSRWAEALRE MSGRLEEMPG DEGYPAYLGS
RLADYYERAG KVVALGKDGR EGAVTAIGAV SPPGGDISEP VTQSTLRIVK VFWGLDAQLA
YKRHFPSINW LTSYSLYLEK MGEWMDAHVA DDWSALRTEA MALLQEEANL EEIVRLVGMD
ALSEGDRLKL EVAKSIREDY LQQNAFHEND TYTSLNKQYK MLNLILSFKH EAEKALEAGV
YLDKVLKLPV RDRIARSKYI SEEEISKMDD ILVELKSEMN KLISEGGVLN A