(data stored in SCRATCH zone)

SWISSPROT: D3VG28_XENNA

ID   D3VG28_XENNA            Unreviewed;       460 AA.
AC   D3VG28;
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 beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347,
GN   ECO:0000313|EMBL:CBJ88118.1};
GN   OrderedLocusNames=XNC1_0025 {ECO:0000313|EMBL:CBJ88118.1};
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:CBJ88118.1, 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:CBJ88118.1, 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 catalytic sites are hosted
CC       primarily by the beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}.
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_01347};
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_01347}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01347}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|HAMAP-Rule:MF_01347}.
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DR   EMBL; FN667742; CBJ88118.1; -; Genomic_DNA.
DR   RefSeq; WP_010846133.1; NC_014228.1.
DR   STRING; 406817.XNC1_0025; -.
DR   EnsemblBacteria; CBJ88118; CBJ88118; XNC1_0025.
DR   KEGG; xne:XNC1_0025; -.
DR   eggNOG; ENOG4105C4J; Bacteria.
DR   eggNOG; COG0055; LUCA.
DR   HOGENOM; HOG000009605; -.
DR   KO; K02112; -.
DR   OMA; FNMIMDG; -.
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   Gene3D; 1.10.1140.10; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VG28.
DR   SWISS-2DPAGE; D3VG28.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01347};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Hydrolase {ECO:0000313|EMBL:CBJ88118.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01347}.
FT   DOMAIN      142    405       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_01347}.
SQ   SEQUENCE   460 AA;  50331 MW;  6C53944AF8760644 CRC64;
     MATGKIIQVI GAVVDVEFPQ DSVPKVYDAL EVKNGEEKLV LEVQQQLGGG IVRCIAMGTS
     DGLRRHLEVT DLGHPIEVPV GKATLGRIMN VLGDPIDMKG EIGEEERWSI HRTAPTYEEL
     SNSQELLETG IKVMDLICPF AKGGKVGLFG GAGVGKTVNM MELIRNIAIE HSGYSVFAGV
     GERTREGNDF YHEMTDSNVL DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL
     FVDNIYRYTL AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTQTGS ITSVQAVYVP
     ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV GQEHYDVARG
     VQSILQRYQE LKDIIAILGM DELSEDDKLV VARARKIQRF LSQPFFVAEV FTGSPGKFVP
     LKDTIRGFKG ILNGDYDHLP EQAFYMVGTI EEAVEKAKKL
//

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