ID ATPB_BURCE STANDARD; PRT; 463 AA. AC P42468; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAY-2006, entry version 39. 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; Burkholderia cepacia complex. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17759 / DSM 50181 / JCM 2799 / NCIB 9085 / NCTC 10661; 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 Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X76877; CAA54204.1; -; Genomic_DNA. DR HSSP; P00829; 1H8E. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR000793; ATPase_a_b_C. DR InterPro; IPR004100; ATPase_a_b_N. DR InterPro; IPR000194; ATPase_a_b_nl-bd. DR InterPro; IPR005722; ATPase_F1_b. DR PANTHER; PTHR15184:SF4; ATP_synthF1_beta; 1. 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; KW Ion transport; Nucleotide-binding; Transport. FT CHAIN 1 463 ATP synthase beta chain. FT /FTId=PRO_0000144429. 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 //