(data stored in SCRATCH zone)

SWISSPROT: ATPB3_PARXL

ID   ATPB3_PARXL             Reviewed;         493 AA.
AC   Q13IW3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   11-DEC-2019, entry version 99.
DE   RecName: Full=ATP synthase subunit beta 3 {ECO:0000255|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta 3 {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta 3 {ECO:0000255|HAMAP-Rule:MF_01347};
GN   Name=atpD3 {ECO:0000255|HAMAP-Rule:MF_01347};
GN   OrderedLocusNames=Bxeno_C0048; ORFNames=Bxe_C0049;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits. {ECO:0000255|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; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
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_01347}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
DR   EMBL; CP000272; ABE35976.1; -; Genomic_DNA.
DR   SMR; Q13IW3; -.
DR   STRING; 266265.Bxe_C0049; -.
DR   EnsemblBacteria; ABE35976; ABE35976; Bxe_C0049.
DR   KEGG; bxb:DR64_8375; -.
DR   KEGG; bxe:Bxe_C0049; -.
DR   PATRIC; fig|266265.5.peg.7829; -.
DR   eggNOG; ENOG4105UHE; Bacteria.
DR   eggNOG; COG0055; LUCA.
DR   HOGENOM; HOG000009605; -.
DR   KO; K02112; -.
DR   OMA; EGHELWH; -.
DR   Proteomes; UP000001817; Chromosome 3.
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; Q13IW3.
DR   SWISS-2DPAGE; Q13IW3.
KW   ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..493
FT                   /note="ATP synthase subunit beta 3"
FT                   /id="PRO_0000339499"
FT   NP_BIND         170..177
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   493 AA;  52453 MW;  A05DBF9E8E793505 CRC64;
     MDTAQPAMTA PPAQAAADEP VGRVTAVRGA VIDVAFDTGA LPMIEDALVI TTDDGQPIIA
     EVQAHLDEGT VRALALRSTN GLRRGAPVRA AGGPIEVPVG EAMLGRLIDV SGVPGDNGTP
     LPPGTPRRPI HRKPPPLASQ GAETRIFATG IKVIDLLTPL AQGGKAAMFG GAGVGKTVLV
     MELIHAMVER YQGISVFAGV GERCREGHEM LTDMRHSGVL PRTVLVYGQM NEPPGARWRV
     PLTALTVAEY FRDERHQNVL LLMDNVFRFV QAGAEVSGLL GRLPSRVGYQ PTLATEVAGL
     QERIVSVGDV SVTAIEAVYV PADDFTDPAV TAIAAHVDSM VVLSRSMAAE GMYPAIDPIA
     SSSVLLDPLV VGGEHARIAI EVRRAVEHYR ELQDVISLLG VEELGADDRR IVGRARRLQR
     FLTQPFAVTE AFTGVPGRSV PVADTLAGCK AILDGNCDDW QESSLYMVGT LDEAREREQA
     TRNAKPVSEH AEP
//

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