(data stored in SCRATCH3701 zone)

SWISSPROT: ATPA1_LISMO

ID   ATPA1_LISMO             Reviewed;         498 AA.
AC   Q8YAM8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 117.
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}; OrderedLocusNames=lmo0090;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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       {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; 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 membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
DR   EMBL; AL591973; CAC98305.1; -; Genomic_DNA.
DR   PIR; AC1086; AC1086.
DR   RefSeq; NP_463623.1; NC_003210.1.
DR   RefSeq; WP_003721716.1; NC_003210.1.
DR   SMR; Q8YAM8; -.
DR   STRING; 169963.lmo0090; -.
DR   PaxDb; Q8YAM8; -.
DR   PRIDE; Q8YAM8; -.
DR   EnsemblBacteria; CAC98305; CAC98305; CAC98305.
DR   GeneID; 986589; -.
DR   KEGG; lmo:lmo0090; -.
DR   PATRIC; fig|169963.11.peg.93; -.
DR   eggNOG; ENOG4108JIN; Bacteria.
DR   eggNOG; COG0056; LUCA.
DR   HOGENOM; HOG000130111; -.
DR   KO; K02111; -.
DR   OMA; ITEGQLY; -.
DR   PhylomeDB; Q8YAM8; -.
DR   BioCyc; LMON169963:LMO0090-MONOMER; -.
DR   Proteomes; UP000000817; 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); IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
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; Q8YAM8.
DR   SWISS-2DPAGE; Q8YAM8.
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..498
FT                   /note="ATP synthase subunit alpha 1"
FT                   /id="PRO_0000238279"
FT   SITE            357
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   498 AA;  55098 MW;  264FD6C0B6B7B6F0 CRC64;
     MKTIHFDMNK YETHVDLEYL KEHGRVEKIS DGVIFCSGLE NAALHQAVLI DERHRGVILE
     LNEEFVGIGL IDKTNDILEG MHVGVSGKFI EVDLFEEMAG RIIDTTGKML YEESEEKPTA
     TSPLFCVTPA IMTIDSVTRP LNTGLAVIDS ITPIGRGQRQ LILGNRQSGK TQIAVDTIIN
     QHDQNVHCIY VAIGLKAAYI AEVIETLRNH GAMEYSTVVA TAASDSLTAQ YLTPYAGMAL
     AEALRDQGKD VLIILDDLTK HADAYRAITL LFNRPPGREA YPGDSFYIHS SLLERAVQMN
     EEHGGGSITA IPMIETLSDD VTAYIPTNVI SITDGQLFLK SDLFNRGQKP AVDVGVSVSR
     IGGDAQHPII RKLSKNLTLI LSQFEELKEL LDFGNALDDG SMKMVSDGRL LTELFKQKIL
     SPLSVTELIV ILYAFQNGFL TKIPPANIQT FKGLLLEKAH MHKDFESFSA QIEAINELNE
     SHVEMLEEII RETGRLFS
//

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