VATA_STRPM
ID VATA_STRPM Reviewed; 591 AA.
AC Q48VL3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=M28_Spy0129;
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180;
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA Lefebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(2005).
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; CP000056; AAX71243.1; -; Genomic_DNA.
DR RefSeq; WP_011284448.1; NC_007296.2.
DR AlphaFoldDB; Q48VL3; -.
DR SMR; Q48VL3; -.
DR EnsemblBacteria; AAX71243; AAX71243; M28_Spy0129.
DR KEGG; spb:M28_Spy0129; -.
DR HOGENOM; CLU_008162_3_1_9; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000009292; 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_1000059358"
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; AC301295D0DD13D7 CRC64;
MNQGKIITVS GPLVVASGMQ EANIQDICRV GHLGLVGEII EMRRDQASIQ VYEETSGIGP
GEPVVTTGCP LSVELGPGLI SEMFDGIQRP LDRFQKATDS DFLIRGVAIP SLDRKAKWAF
IPKLSVGQEV VAGDILGTVQ ETAVIEHRIM VPYKVSGTLV AIHAGDFTVT DTVYEIKKED
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