ATPA_VIBAL
ID ATPA_VIBAL Reviewed; 513 AA.
AC P12985;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; Synonyms=uncA;
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=138-2;
RX PubMed=2529481; DOI=10.1093/nar/17.19.7993;
RA Krumholz L.R., Esser U., Simoni R.D.;
RT "Nucleotide sequence of the unc operon of Vibrio alginolyticus.";
RL Nucleic Acids Res. 17:7993-7994(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-19.
RC STRAIN=138-2;
RX PubMed=2532151; DOI=10.1016/0014-5793(89)81657-6;
RA Dmitirev O.Y., Grinkevich V.A., Skulachev V.P.;
RT "The F1-ATPase of Vibrio alginolyticus. Purification and N-terminal
RT sequence of major subunits.";
RL FEBS Lett. 258:219-222(1989).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
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_01346};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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; X16050; CAA34179.1; -; Genomic_DNA.
DR PIR; S06080; S06080.
DR AlphaFoldDB; P12985; -.
DR SMR; P12985; -.
DR STRING; 663.BAU10_15090; -.
DR PRIDE; P12985; -.
DR eggNOG; COG0056; Bacteria.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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 CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..513
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144364"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 373
FT /note="Required for activity"
SQ SEQUENCE 513 AA; 55591 MW; A31BD99FCD1E7CE6 CRC64;
MQLNSTEISD LIKQRIESFE VVSEARNEGT IVSVSDGIIR IHGLADVMQG EMIELPGGRY
ALALNLERDS VGAVVMGPYA DLKEGMKVTG TGRILEVPVG PELLGRVVNT LGEPIDGKGP
IEAKMTSPVE VIAPGVIDRK SVDQPVQTGY KSVDSMIPIG RGQRELIIGD RQIGKTALAI
DAIINQKDSG IFSIYVAIGQ KASTIANVVR KLEEHGALQN TIVVVASASE SAALQYLAPY
AGCAMGEYFR DRGEDALIVY DDLSKQAVAY RQISLLLKRP PGREAFPGDV FYLHSRLLER
AARVNEEYVE RFTNGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLQTELF
NAGVRPAVDP GISVSRVGGS AQTKIIKKLS GGIRTALAAY RELAAFAQFS SDLDEATKKQ
LDHGQKVTEL MKQKQYAPMS VFDQALTIFA AERGYLDDVE LNKVLDFEAA LLSYARGQYA
ELAAEIDKSG AYNDEIEAQL KKLTDDFKAT QTW
