(data stored in ACNUC10821 zone)

SWISSPROT: ATPA1_LISMF

ID   ATPA1_LISMF             Reviewed;         498 AA.
AC   Q724W6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=ATP synthase subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01346};
GN   Name=atpA1 {ECO:0000255|HAMAP-Rule:MF_01346}; Synonyms=atpA-1;
GN   OrderedLocusNames=LMOf2365_0107;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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 three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains. {ECO:0000255|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell 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; AE017262; AAT02895.1; -; Genomic_DNA.
DR   RefSeq; WP_003728365.1; NC_002973.6.
DR   SMR; Q724W6; -.
DR   PRIDE; Q724W6; -.
DR   EnsemblBacteria; AAT02895; AAT02895; LMOf2365_0107.
DR   KEGG; lmf:LMOf2365_0107; -.
DR   HOGENOM; HOG000130111; -.
DR   KO; K02111; -.
DR   OMA; KFPSYNE; -.
DR   BioCyc; LMON265669:G1G0V-107-MONOMER; -.
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   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; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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   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; Q724W6.
DR   SWISS-2DPAGE; Q724W6.
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN         1    498       ATP synthase subunit alpha 1.
FT                                /FTId=PRO_0000238281.
FT   SITE        357    357       Required for activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01346}.
SQ   SEQUENCE   498 AA;  55142 MW;  508A702301BE366A CRC64;
     MKTIHFDMNK YETHVDLEYL KEHGRVEKIS DGVIFCSGLE NAALHQAVLI DERHRGVILE
     LNEEFVGIGL IDKTNDILEG MHVGVSGKFI EVDLFEEMAG RVIDTTGKML YEESEEKPTA
     TSPLFCVTPA IMTIDSVTRP LNTGLAVIDS ITPIGRGQRQ LILGNRQSGK TQIAVDTIIN
     QHDQNVHCIY VAIGLKAAYI AEVIETLRNH GAMEYSTVVA TAASDSLTAQ YLTPYAGMAV
     AEALRDQGKD VLIILDDLTK HADAYRAITL LFNRPPGREA YPGDSFYIHS SLLERAVQMN
     EEHGGGSITA IPMIETLSDD VTAYIPTNVI SITDGQLFLK SDLFNRGQKP AVDVGVSVSR
     IGGDAQHPII RKLSKNLTLI LSQFEELKEL LDFGNALDDG SMKMVSDGRL LTELFKQKIL
     SPLSVTELIV ILYAFQNGFL TKIPPANIQT FKDLLLEKAH MHKDFESFSA QIETINELNE
     SHIEMLEEII REAGRLFS
//

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