ID ATPD_BRUA2 Reviewed; 186 AA. AC Q2YLI4; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; GN OrderedLocusNames=BAB1_1810; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence CC of a proton or sodium gradient. F-type ATPases consist of two CC structural domains, F(1) containing the extramembraneous catalytic core CC and F(0) containing the membrane proton channel, linked together by a CC central stalk and a peripheral stalk. During catalysis, ATP synthesis CC in the catalytic domain of F(1) is coupled via a rotary mechanism of CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). CC It either transmits conformational changes from CF(0) to CF(1) or is CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core CC - and F(0) - the membrane proton channel. F(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an CC alternating ring which encloses part of the gamma chain. F(1) is CC attached to F(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_01416}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01416}. 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; AM040264; CAJ11766.1; -; Genomic_DNA. DR RefSeq; WP_002964879.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YLI4; -. DR SMR; Q2YLI4; -. DR STRING; 359391.BAB1_1810; -. DR GeneID; 3788633; -. DR KEGG; bmf:BAB1_1810; -. DR PATRIC; fig|359391.11.peg.320; -. DR HOGENOM; CLU_085114_0_1_5; -. DR PhylomeDB; Q2YLI4; -. DR Proteomes; UP000002719; Chromosome I. 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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf. DR InterPro; IPR020781; ATPase_OSCP/d_CS. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR NCBIfam; TIGR01145; ATP_synt_delta; 1. DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1. DR PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1..186 FT /note="ATP synthase subunit delta" FT /id="PRO_0000370909" SQ SEQUENCE 186 AA; 19648 MW; DA7DD5340AAAAF41 CRC64; MAETSSLISG VAQRYAGSLF EHALDANSVA SVEKDLGRFE ALLSGSEDLR RLISSPVFSS EDQLHAIGAI ADKAGIKGLV GNFLRVVAQN RRLFALPGII AAFRQIAAEH RGEISADVVS AHELTSAQQN ELKATLKGVA GKDVTINVTV DPSILGGLIV KMGSRQIDTS LRTKLSSLKL ALKEVG //