VATA_SULIN
ID VATA_SULIN Reviewed; 592 AA.
AC C3NGV1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=YN1551_1266;
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The archaeal 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; CP001404; ACP48361.1; -; Genomic_DNA.
DR RefSeq; WP_012717392.1; NC_012623.1.
DR AlphaFoldDB; C3NGV1; -.
DR SMR; C3NGV1; -.
DR EnsemblBacteria; ACP48361; ACP48361; YN1551_1266.
DR GeneID; 7810925; -.
DR KEGG; sin:YN1551_1266; -.
DR HOGENOM; CLU_008162_3_1_2; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000006818; Chromosome.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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; IPR005726; ATP_synth_asu_arc.
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 TIGRFAMs; TIGR01043; ATP_syn_A_arch; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..592
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000205036"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 592 AA; 66455 MW; 002B834BC5F9D6AD CRC64;
MNNGRIVRIN GPLVVADNMK NAQMYEVVEV GEPRLIGEIT RIEGDRAFIQ VYEDTSGIKP
NEPVYRTGAP LSIELGPGLI GKIFDGLQRP LDSIKELTKS PFIARGIKVP SVDRKTKWHF
IPKVKKGDKI EGGDIIGIVN ETPLVEHRIL VPPYVHGTLK EIVAEGDYTV EDPIAVVDMN
GDEVPIRLMQ RWPVRIPRPF REKLEPTEPL LTGTRVLDTI FPIAKGGTAA IPGPFGSGKT
VTLQSLAKWS AAKIVIYVGC GERGNEMTDE LRQFPSLKDP WTGRPLLERT ILVANTSNMP
VAAREASIYV GITMAEYFRD QGYDTLLVAD STSRWAEALR DLGGRMEEMP AEEGFPSYLP
SRLAEYYERA GRVKTVGKPE RFGSVTVASA VSPPGGDFTE PVTSQTLRFV KVFWPLDVSL
AQARHYPAIN WLQGFSAYVD LVANWWNTNV DPKWREMRDM MVRTLIREDE LRQIVRLVGP
ESLAEKDKLV LETARLIKEA FLKQNAYDDI DAFSSPQKQA RVMRLIYLFN THASRLVERG
IPTKKIVDSM GQLLPEIIRS KAAIKNDELN KYDELERKLI SVFENLEKEA GT