VATA_ANAD2
ID VATA_ANAD2 Reviewed; 579 AA.
AC B8JE35;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=A2cp1_2763;
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) 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.
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; CP001359; ACL66100.1; -; Genomic_DNA.
DR RefSeq; WP_012633861.1; NC_011891.1.
DR AlphaFoldDB; B8JE35; -.
DR SMR; B8JE35; -.
DR EnsemblBacteria; ACL66100; ACL66100; A2cp1_2763.
DR KEGG; acp:A2cp1_2763; -.
DR HOGENOM; CLU_008162_3_1_7; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000007089; 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; 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.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..579
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000132880"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 579 AA; 61608 MW; 33F12DD3B372A54A CRC64;
MSGTLMRMAG PTVVAEGLSG ASLNEVVRVG EERLLGEIIR IEGDRATIQV YEETAGLALG
EPVEASGEPL AVELGPGLLG SVFDGVQRPL SELAAREGDF LGRGASLPAL DRTRAWEFEP
AVAPGDRVEG GARLGVARAP GAPDHPVVVP PGVTGRVAEV RGGARRVDEP AVLLEGGATL
ALLERWPVRR PRPARRRLPP DVPFLTGQRV LDCFFPVSAG GTAVVPGGFG TGKTVLEQSL
AKWAAADVVV YVGCGERGNE MSEVLDEFPR LEDPRTGGPL LARTVMIVNT SNMPVAAREA
SIYTGCAIAE YFRDMGRSVA LMIDSTSRWA EALREISARL EEMPGEEGYP TYLASRLARF
YERAGRVETL GGAEGAVTMV GAVSPPGGDL SEPVTQCSLR ATGALWALSA DLAHRRHYPA
VDWSVSFTLE GDRLAGWFER EAGDGFGALR DEARKLLQRE RELAEVAELV GTESLQDAER
LVLESARLLR EGFLRQSALD PADATCPPAK AFEMLRLFLE WHRRAGAAVG AGVPLRSILD
TGLGARLLRL AQLPAAEVPG AAAALRADLS EALARLEAE