VATA_STRPF
ID VATA_STRPF Reviewed; 591 AA.
AC Q1J8S5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=MGAS10750_Spy0136;
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(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}.
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DR EMBL; CP000262; ABF37086.1; -; Genomic_DNA.
DR RefSeq; WP_010921823.1; NC_008024.1.
DR AlphaFoldDB; Q1J8S5; -.
DR SMR; Q1J8S5; -.
DR EnsemblBacteria; ABF37086; ABF37086; MGAS10750_Spy0136.
DR KEGG; spi:MGAS10750_Spy0136; -.
DR HOGENOM; CLU_008162_3_1_9; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000002434; 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; Translocase; Transport.
FT CHAIN 1..591
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000059356"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 591 AA; 64967 MW; DBF74909A6964961 CRC64;
MNQGKIITVS GPLVVASGMQ EANIQDICRV GHLGLVGEII EMRRDQASIQ VYEETSGIGP
GEPVVTTGCP LSVELGPGLI SEMFDGIQRP LDRFQKATDS DFLIRGVAIP SLDRKAKWAF
IPKLSVGQEV VAGDILGTVQ ETAVIEHRIM VPYKVSGTLV AIHAGDFTVT DTVYEIKQED
GSIYQGSLMQ TWPVRQSRPV AQKLIPVEPL VTGQRVIDTF FPVTKGGAAA VPGPFGAGKT
VVQHQIAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP NTGQSIMERT VLIANTSNMP
VAAREASIYT GITIAEYFRD MGYSVAIMAD STSRWAEALR EMSGRLQEMP GDEGYPAYLG
SRIAEYYERA GRVRTLGSQE REGTITAIGA VSPPGGDISE PVTQNTLRIV KVFWGLDAPL
AQRRHFPAIN WLTSYSLYQD DVGSYIDRKQ QSNWSNKVTR AMAILQREAS LEEIVRLVGL
DSLSEQDRLT MAVARQIRED YLQQNAFDSV DTFTSFPKQE AMLTNILTFN EEASKALSLG
AYFNEIMEGT AQVRDRIARS KFIPEENLEQ IKGLTQKVTK EIHHVLAKGG I