ATPB_PAEAT
ID ATPB_PAEAT Reviewed; 483 AA.
AC A1R7V3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATP synthase subunit beta {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 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=AAur_2594;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(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 membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM06774.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000474; ABM06774.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014922173.1; NC_008711.1.
DR AlphaFoldDB; A1R7V3; -.
DR SMR; A1R7V3; -.
DR STRING; 290340.AAur_2594; -.
DR EnsemblBacteria; ABM06774; ABM06774; AAur_2594.
DR KEGG; aau:AAur_2594; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_11; -.
DR OrthoDB; 430176at2; -.
DR Proteomes; UP000000637; 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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..483
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000339474"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 483 AA; 52339 MW; 48A60AFF7B374251 CRC64;
MTATATEHVA TAGATGRIAR VIGPVVDVEF PADAIPSIYN ALTTEITLNG QTKTITFETS
QHLGDNLVRA ISLQATDGLV RGTTVQDSGA PISVPVGDGV KGHIFNVLGK PLDVEESEIK
ADAYWPIHRK APSFASLEGS TEMLETGIKV IDLLTPYIKG GKIGLFGGAG VGKTVLIQEM
ITRVARNFGG TSVFAGVGER TREGNDLWVE MEEAGVLKDT ALVFGQMDEP PGTRLRVALS
ALTMAEYFRD VQNQDVLLFI DNIFRFTQAG SEVSTLLGRM PSAVGYQPNL ADEMGLLQER
ITSTKGHSIT SMQAIYVPAD DYTDPAPATT FAHLDATTEL SREIASRGLY PAVDPLTSTS
RILDPQYIGK DHYNTAVRVK QILQKNKELQ DIIAILGVDE LSEEDKIVVS RARRIQQFLS
QNTYTAKQFT GVEGSTVSIK DTVEGFTAIC DGELDHIAEQ AFFNVGGLDD VERNWAKIQE
QTK
