(data stored in ACNUC1104 zone)

SWISSPROT: D3VG30_XENNA

ID   D3VG30_XENNA            Unreviewed;       513 AA.
AC   D3VG30;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 54.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346,
GN   ECO:0000313|EMBL:CBJ88120.1};
GN   OrderedLocusNames=XNC1_0027 {ECO:0000313|EMBL:CBJ88120.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88120.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88120.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|HAMAP-Rule:MF_01346}.
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DR   EMBL; FN667742; CBJ88120.1; -; Genomic_DNA.
DR   RefSeq; WP_010846131.1; NC_014228.1.
DR   STRING; 406817.XNC1_0027; -.
DR   EnsemblBacteria; CBJ88120; CBJ88120; XNC1_0027.
DR   KEGG; xne:XNC1_0027; -.
DR   eggNOG; ENOG4105CDG; Bacteria.
DR   eggNOG; COG0056; LUCA.
DR   HOGENOM; HOG000130111; -.
DR   KO; K02111; -.
DR   OMA; GNAQIKS; -.
DR   Proteomes; UP000008075; 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   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; D3VG30.
DR   SWISS-2DPAGE; D3VG30.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01346};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Hydrolase {ECO:0000313|EMBL:CBJ88120.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   DOMAIN       29     92       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      149    375       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      382    507       ATP-synt_ab_C. {ECO:0000259|Pfam:
FT                                PF00306}.
FT   NP_BIND     169    176       ATP. {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   SITE        373    373       Required for activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01346}.
SQ   SEQUENCE   513 AA;  55467 MW;  D04F57A74BBDB6BF CRC64;
     MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVNDGIIR VHGLADVMQG EMISLPGNRY
     AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG RGLLGRVVNT LGEPIDGKGA
     VEHDGFSPVE VIAPGVIDRQ SVDQPVQTGY KSVDAMIPIG RGQRELVIGD RQTGKTALAI
     DAIINQRNSG IKCIYVAIGQ KASTISNVVR KLEEHGALEN TIVVVASASE SAALQYLAPY
     SGCAMGEYFR DRGEDALIVY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER
     AARVNAEYVE KFTNGEVKGQ TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLESSLF
     NAGIRPAVNP GISVSRVGGA AQTKIIKKLS GGIRTALAQY RELAAFSQFA SDLDDATRKQ
     LDHGQKVTEL LKQKQYLPMS IAQQALSLFA AERGYLEDVE IAKVVSFEAA LLAYASREHS
     DFLKEIDQSG DYNGEIEAKL KALLESFKAT QSW
//

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