ATPA_RHOCA
ID ATPA_RHOCA Reviewed; 509 AA.
AC P72245;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
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 Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9440534; DOI=10.1128/jb.180.2.416-421.1998;
RA Borghese R., Crimi M., Fava L., Melandri B.A.;
RT "The ATP synthase atpHAGDC (F1) operon from Rhodobacter capsulatus.";
RL J. Bacteriol. 180:416-421(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-20, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=GA;
RA Gabellini N., Gao Z., Eckerskorn C., Lottspeich F., Oesterhelt D.;
RT "Purification of the H+-ATPase from Rhodobacter capsulatus, identification
RT of the F1F0 components and reconstitution of the active enzyme.";
RL Biochim. Biophys. Acta 934:227-234(1988).
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). {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|Ref.2}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01346, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; X99599; CAA67908.1; -; Genomic_DNA.
DR RefSeq; WP_013068673.1; NZ_VIBE01000018.1.
DR AlphaFoldDB; P72245; -.
DR SMR; P72245; -.
DR PRIDE; P72245; -.
DR GeneID; 31491768; -.
DR OMA; LQAPGVM; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore 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 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; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..509
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144345"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 369
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 509 AA; 54864 MW; F64737C5A6D37E8E CRC64;
MGIQAAEISA ILKEQIKNFG QDAQVAEVGR VLSVGDGIAR VHGLDNVQAG EMVEFPGGIR
GMALNLEVDN VGIVIFGSDR DIKEGDTVKR TNAIVDVPAG EGLLGRVVDG LGNPIDGKGP
IVAKERRIAD VKAPGIIPRK SVHEPMATGL KSVDAMIPIG RGQRELIIGD RQTGKTAIAL
DTILNQKSYN DANPGNKLHC FYVAIGQKRS TVAQLVKKLE EAGAMEYTTV VAATASDPAP
MQFLAPYSAT AMAEYFRDNG MHALIIYDDL SKQAVAYRQM SLLLRRPPGR EAYPGDVFYL
HSRLLERSAK LNEDFGSGSL TALPVIETQG GDVSAFIPTN VISITDGQIF LETELFYQGI
RPAVNTGLSV SRVGSSAQTN SMKSVAGPVK LELAQYREMA AFAQFGSDLD AATQKLLNRG
ARLTELMKQP QYSPLTNAEI VAVIFAGTNG FLDAVPVKEV GRFEKGLLAY LRSTRKDVLE
WLTKEDPKIK GDAEKKLKDA IAEFAKTFA
