ID ATPB_RICFE Reviewed; 474 AA. AC Q4UK18; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 24-JAN-2024, entry version 119. 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}; GN OrderedLocusNames=RF_1266; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAY62117.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000053; AAY62117.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; Q4UK18; -. DR SMR; Q4UK18; -. DR STRING; 315456.RF_1266; -. DR KEGG; rfe:RF_1266; -. DR eggNOG; COG0055; Bacteria. DR HOGENOM; CLU_022398_0_2_5; -. DR OrthoDB; 9801639at2; -. DR Proteomes; UP000008548; 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; ATP-binding; Cell inner membrane; Cell membrane; CF(1); KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding; KW Translocase; Transport. FT CHAIN 1..474 FT /note="ATP synthase subunit beta" FT /id="PRO_0000254363" FT BINDING 153..160 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347" SQ SEQUENCE 474 AA; 51191 MW; A70DFF2D9040B16A CRC64; MTKNIGKITQ IISAVVDVKF TNNGELPEIL NALECYNDKQ RIVLEVAQHI GDDTVRCIAM DSTEGLVRGV EVIDTGSPIR IPVGTETLGR IMNVVGEPID GKGDIKSSNI SSIYKSAPDF TNQSTERNIL VTGIKVVDLL APYTKGGKIG LFGGAGVGKT VLIMELINNV AKAHGGYTVF AGVGERTREG NDLYHEMIDS GVIDLEKPEN SKVALVYGQM NEPPGARARV ALSGLTIAES FRDMNEGQDV LFFVDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGE LQERITSTKN GSITSVQAIY VPADDLTDPA PATSFAHLDA TTVLSRQIAE LGIYPAVDPL DSNSQVLDPM IVGEEHYSVA RQVQQILQTY KSLQDIIAIL GMDELSEEDK LTVSRARKIQ RFLSQPFHVA EVFTGAEGKF VNLADTIAGF KGLVEGKYDD LPEAAFYMVG TMDEAIEKAK ILKG //