ID   VATA_CLOD6              Reviewed;         592 AA.
AC   Q184E7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=CD630_29560;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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}.
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; AM180355; CAJ69848.1; -; Genomic_DNA.
DR   RefSeq; WP_003426762.1; NZ_CP010905.2.
DR   RefSeq; YP_001089472.1; NC_009089.1.
DR   AlphaFoldDB; Q184E7; -.
DR   SMR; Q184E7; -.
DR   STRING; 272563.CD630_29560; -.
DR   EnsemblBacteria; CAJ69848; CAJ69848; CD630_29560.
DR   GeneID; 66355362; -.
DR   KEGG; cdf:CD630_29560; -.
DR   KEGG; pdc:CDIF630_03239; -.
DR   PATRIC; fig|272563.120.peg.3122; -.
DR   eggNOG; COG1155; Bacteria.
DR   OMA; RIVKTFW; -.
DR   PhylomeDB; Q184E7; -.
DR   BioCyc; PDIF272563:G12WB-3120-MON; -.
DR   Proteomes; UP000001978; 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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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..592
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000322463"
FT   BINDING         232..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   592 AA;  65526 MW;  EA32CAD099CE02F6 CRC64;
     MKTGTIVKVS GPLVVAEGMR DANMFDVVRV SDKHLIGEII EMHGDKASIQ VYEETSGLGP
     GEEVVSLGMP MSVELGPGLI STIYDGIQRP LEKMYDISGT NITKGVEVSS LDRTTKWEFK
     PKKSVGDKVV AGDIIGGVQE TAVVECKIMV PYGVKGTIKE IYSGEFTVED TVCVITDEKG
     NDIPVTMMQK WPVRKERPYR EKKTPDSLLV TGQRVIDTFF PITKGGVAAI PGPFGSGKTV
     TQHQLAKWAD ADIVVYIGCG ERGNEMTDVL LEFPELKDPR TGESLMQRTV LIANTSDMPV
     AAREASIYTG ITIAEYFRDM GYSVALMADS TSRWAEALRE MSGRLEEMPG EEGYPAYLGS
     RLAQFYERAG KVNCLGMDER EGTLTAIGAV SPPGGDTSEP VSQATLRIVK VFWGLDASLA
     YKRHFPAINW LTSYSLYQEK VDVWADKNVN DNFSAQRAQA MKLLQVESEL QEIVQLVGVD
     SLSDGDRLIL EVTRSIREDF LHQNSFHEVD TYTSLHKQYR MMGLILKFYK SAQDAIKQNV
     TINDIIKLSV LEKIGRAKYV EEGDIDAAYD SIEDEIDNEL ADLIKKRGAE EL