ID   ATPB_BURCE     STANDARD;      PRT;   463 AA.
AC   P42468;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   ATP synthase beta chain (EC 3.6.3.14).
GN   Name=atpD;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 50181;
RX   MEDLINE=94368062; PubMed=8085791;
RA   Ludwig W., Neumaier J., Klugbauer N., Brockmann E., Roller C.,
RA   Klugbauer S., Reetz K., Schachtner I., Ludvigsen A., Bachleitner M.,
RA   Fischer U., Schleifer K.H.;
RT   "Phylogenetic relationships of Bacteria based on comparative sequence
RT   analysis of elongation factor Tu and ATP-synthase beta-subunit
RT   genes.";
RL   Antonie Van Leeuwenhoek 64:285-305(1993).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The beta chain is the catalytic
CC       subunit.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
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, b and c.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X76877; CAA54204.1; -.
DR   HSSP; P00829; 1H8E.
DR   InterPro; IPR003593; AAA_ATPase.
DR   InterPro; IPR005722; ATP_synthF1_beta.
DR   InterPro; IPR000793; ATPase_a/b_C.
DR   InterPro; IPR004100; ATPase_a/b_N.
DR   InterPro; IPR000194; ATPase_a/bcentre.
DR   InterPro; IPR009005; F1_ATPase_a/b_N.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
KW   ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Hydrolase.
FT   NP_BIND     153    160       ATP (By similarity).
SQ   SEQUENCE   463 AA;  50539 MW;  E0CF51515A382E30 CRC64;
     MSTAALVEGK IVQCIGAVID VEFPRDSMPK IYDALILDGS ELTLEVQQQL GDGVVRTICL
     GASDGLRRGL TVKNTSKPIS VPVGKPTLGR IMDVLGRPID EAGPIESEHT RSIHQKAPAF
     DELSPSTELL ETGIKVIDLI CPFAKGGKVG LFGGAGVGKT VNMMELINNI AKEHGGYSVF
     AGVGERTREG NDFYHEMKDS NVLDKVALVY GQMNEPPGNR LRVLTGLTMA EHFRDEGLDV
     LFFVDNIYRF TLAGTEVSAL LGRMPSAVGY QPTLAEEMGK LQERITSTKK GSITSVQAVY
     VPADDLTDPS PATTFGHLDA TVVLSRDIAS LGIYPAVDPL DSTSRQIDPN VIGEEHYSIT
     RRVQQTLQRY KELRDIIAIL GMDELSPEDK LSVARARKIQ RFLSQPFHVA EVFTGSPGKY
     VPLKETIRGF KMIVDGECDH LPEQAFYMVG TIDEAFEKAK KIS
//