ID D9QIE3_BRESC Unreviewed; 519 AA.
AC D9QIE3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Bresu_0131 {ECO:0000313|EMBL:ADK99445.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADK99445.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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: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; EC=7.1.2.2;
CC Evidence={ECO:0000256|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:0000256|HAMAP-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|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
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DR EMBL; CP002102; ADK99445.1; -; Genomic_DNA.
DR RefSeq; WP_013267550.1; NC_014375.1.
DR AlphaFoldDB; D9QIE3; -.
DR STRING; 633149.Bresu_0131; -.
DR KEGG; bsb:Bresu_0131; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_5; -.
DR InParanoid; D9QIE3; -.
DR OrthoDB; 9801639at2; -.
DR BioCyc; BSUB633149:G1GM8-131-MONOMER; -.
DR Proteomes; UP000002696; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01347}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01347}; Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT DOMAIN 183..392
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ SEQUENCE 519 AA; 55136 MW; FB1988E793671447 CRC64;
MTDTVAPKKP AAPRKPKAPV APAAASATGN AAYTAGTGVG KIAQVIGAVV DVEFTGQLPA
ILNALETQNV DQKTGEPFTL VLEVAQHLGE NMVRAISMDT TEGLTRGQPV TDTGTSILAP
VGPGTLGRIM NVVGAPIDEQ GPIATTMYRP IHREAPTFEE QSTSSEILVT GIKVIDLICP
YTKGGKIGLF GGAGVGKTVT MQELINNIAK AYGGYSVLAG VGERTREGND LYHEMIESNV
NVDPSKNGGS TEGSKCALVY GQMNEPPGAR ARVALTGLAQ AEYFRDEEGK DVLLFVDNIF
RFTQAGSEVS ALLGRIPSAV GYQPTLATEM GNLQERITST KKGSITSVQA IYVPADDLTD
PAPAASFAHL DATTVLNRDI AAQAIFPAVD PLDSTSRIMD PLVIGEEHYL VARSVQEVLQ
QYKALKDIIA ILGMDELSEE DKLIVSRARK IQRFLSQPFF VAEQFTNSPG KFVELADTIR
SFKGIVAGEY DHLPEAAFYM VGPIEEAVEK AQKLAADAA
//
