ATPA_RHORU
ID ATPA_RHORU Reviewed; 510 AA.
AC P05036;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 136.
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};
OS Rhodospirillum rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=1085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2861810; DOI=10.1042/bj2280391;
RA Falk G., Hampe A., Walker J.E.;
RT "Nucleotide sequence of the Rhodospirillum rubrum atp operon.";
RL Biochem. J. 228:391-407(1985).
RN [2]
RP PROTEIN SEQUENCE OF 1-15.
RX PubMed=1327870; DOI=10.1016/0014-5793(92)81326-h;
RA Andralojc P.J., Harris D.A.;
RT "Isolation and characterisation of a functional alpha beta heterodimer from
RT the ATP synthase of Rhodospirillum rubrum.";
RL FEBS Lett. 310:187-192(1992).
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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12) (By similarity). {ECO:0000250}.
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; X02499; CAA26338.1; -; Genomic_DNA.
DR PIR; S08581; PWQFA.
DR RefSeq; WP_011388979.1; NZ_NHSM01000086.1.
DR AlphaFoldDB; P05036; -.
DR SMR; P05036; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:CACAO.
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:0006754; P:ATP biosynthetic process; IDA:CACAO.
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 PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 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..510
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144346"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 371
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 510 AA; 55026 MW; B3212647074D3F91 CRC64;
MEIRAAEISA ILKEQIANFG TEAESAEVGQ VLSVGDGIAR VYGLDNVQAG EMVEFANGVK
GMALNLESDN VGIVIFGEDR GIKEGDVVKR TQTIVDVPVG KGLLGRVVDG LGNPIDGKGD
LVDVERKRAE VKAPGIIPRK SVHEPVQTGI KAIDSLIPIG RGQRELIIGD RQTGKTAVIL
DTILNQKAVN DKAKDDSEKL FCVYVAVGQK RSTVAQVVKV LADHGALDYT IVVAATASEP
APLQFLAPYT GCTMGEFFRD NGMHAVIFYD DLTKQAVAYR QMSLLLRRPP GREAFPGDVF
YLHSRLLERA AKLNDDNGAG SLTALPVIET QANDVSAYIP TNVISITDGQ IFLETDLFFK
GIRPAVNVGL SVSRVGSSAQ IKAMKQVAGS IKLELAQYRE MAAFAQFASD LDPATQKLLA
RGARLTELLK QAQYSPLAVE EQVCVIYAGT RGYLDKLKTT DVVRYEASLL GALRTSGADL
LESIRTGKAL SKEIEQKLVK FLDDFGKKFA
