(data stored in ACNUC7421 zone)

SWISSPROT: ATPA_RHOPS

ID   ATPA_RHOPS              Reviewed;         510 AA.
AC   Q13DP4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
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};
GN   OrderedLocusNames=RPD_0557;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The alpha chain is a regulatory
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01346}.
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;
CC         EC=7.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has four main subunits: a(1), b(1), b'(1) and c(9-12) (By
CC       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}.
DR   EMBL; CP000283; ABE37795.1; -; Genomic_DNA.
DR   RefSeq; WP_011500982.1; NC_007958.1.
DR   SMR; Q13DP4; -.
DR   STRING; 316057.RPD_0557; -.
DR   PRIDE; Q13DP4; -.
DR   EnsemblBacteria; ABE37795; ABE37795; RPD_0557.
DR   KEGG; rpd:RPD_0557; -.
DR   eggNOG; ENOG4105CDG; Bacteria.
DR   eggNOG; COG0056; LUCA.
DR   HOGENOM; HOG000130111; -.
DR   KO; K02111; -.
DR   OMA; GNAQIKS; -.
DR   OrthoDB; 837522at2; -.
DR   BioCyc; RPAL316057:RPD_RS02860-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 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   3: Inferred from homology;
DR   PRODOM; Q13DP4.
DR   SWISS-2DPAGE; Q13DP4.
KW   ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW   Complete proteome; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN         1    510       ATP synthase subunit alpha.
FT                                /FTId=PRO_0000302694.
FT   NP_BIND     169    176       ATP. {ECO:0000255|HAMAP-Rule:MF_01346}.
FT   SITE        371    371       Required for activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01346}.
SQ   SEQUENCE   510 AA;  55158 MW;  0C06CCC182CEB3AE CRC64;
     MDIRAAEISA ILKDQIKNFG QEAEVTEVGQ VLSVGDGIAR VYGLDNVLAG EMVEFENGTR
     GMALNLETDN VGIVIFGADR EIKEGQTVKR TRSIVDTPVG KGLLGRVVDA LGNPIDGKGP
     IQATERKRVD VKAPGIIPRK SVNEPMATGL KAIDALIPVG RGQRELIIGD RQTGKTAIAL
     DTILNQKPLN VEGAPEGQKL YCVYVAVGQK RSTVAQFVKV LEEQGALEYS IVVAATASDP
     APMQYIAPFT GCTMGEYFRD NGMHAVIIYD DLSKQAVAYR QMSLLLRRPP GREAYPGDVF
     YLHSRLLERA AKLNEDHGSG SLTALPIIET QANDVSAYIP TNVISITDGQ IFLETDLFFQ
     GIRPAVNVGL SVSRVGSSAQ TKAMKKVAGK IKGELAQYRE MAAFAQFGSD LDASTQRLLN
     RGSRLTELLK QPQFSPLKME EQVVVIYAGV NGYLDALPVA KVRSFEDGLL SLLRGKESAI
     LDAIRTSRDL SDDTAAKLKA VIESYAKTFA
//

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