ID A0A3A3JZ35_SALMO Unreviewed; 177 AA. AC A0A3A3JZ35; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 16-JAN-2019, entry version 2. DE RecName: Full=ATP synthase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416}; DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416}; DE AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416}; DE Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416}; GN Name=atpH {ECO:0000256|HAMAP-Rule:MF_01416}; GN ORFNames=D5G08_20540 {ECO:0000313|EMBL:RJH05479.1}, D5G10_20765 GN {ECO:0000313|EMBL:RJG93003.1}, D5G13_18235 GN {ECO:0000313|EMBL:RJG81303.1}, D5G14_19295 GN {ECO:0000313|EMBL:RJG95937.1}, D5G16_19120 GN {ECO:0000313|EMBL:RJH86006.1}, D5G21_18210 GN {ECO:0000313|EMBL:RJH27381.1}, D5G48_14875 GN {ECO:0000313|EMBL:RJI65542.1}, D5G49_19080 GN {ECO:0000313|EMBL:RJI69663.1}; OS Salmonella montevideo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=115981 {ECO:0000313|EMBL:RJH05479.1}; RN [1] {ECO:0000313|EMBL:RJH05479.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10TTU284x {ECO:0000313|EMBL:RJG81303.1}, 10TTU450x RC {ECO:0000313|EMBL:RJG95937.1}, 10TTU89b1 RC {ECO:0000313|EMBL:RJG93003.1}, 11TTU100TT RC {ECO:0000313|EMBL:RJH05479.1}, 11TTU1258b RC {ECO:0000313|EMBL:RJH27381.1}, 11TTU2168x RC {ECO:0000313|EMBL:RJH86006.1}, 11TTUT490TT RC {ECO:0000313|EMBL:RJI65542.1}, and 11TTUT642TT RC {ECO:0000313|EMBL:RJI69663.1}; RA Bugarel M., Cook P.W., Harris S.L., Harhay D.M., Den Bakker H.C., RA Nightingale K., Loneragan G.H.; RT "Phenotypic and genotypic characterization of Salmonella enterica sp. RT enterica Lubbock supports this new serotype evolved from a Salmonella RT Mbandaka progenitor strains followed by recombination events with RT Salmonella Montevideo."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000256|HAMAP-Rule:MF_01416}. CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CC CF(1). It either transmits conformational changes from CF(0) to CC CF(1) or is implicated in proton conduction. {ECO:0000256|HAMAP- CC Rule:MF_01416}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01416}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000256|HAMAP-Rule:MF_01416, ECO:0000256|SAAS:SAAS01082575}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RJH05479.1}. 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; QYVL01000020; RJG81303.1; -; Genomic_DNA. DR EMBL; QYVR01000024; RJG93003.1; -; Genomic_DNA. DR EMBL; QYVP01000020; RJG95937.1; -; Genomic_DNA. DR EMBL; QYVT01000019; RJH05479.1; -; Genomic_DNA. DR EMBL; QYVW01000032; RJH27381.1; -; Genomic_DNA. DR EMBL; QYWL01000041; RJH86006.1; -; Genomic_DNA. DR EMBL; QYXA01000035; RJI65542.1; -; Genomic_DNA. DR EMBL; QYXB01000037; RJI69663.1; -; Genomic_DNA. DR RefSeq; WP_001288957.1; NZ_UGVP01000002.1. DR Gene3D; 1.10.520.20; -; 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 PANTHER; PTHR11910; PTHR11910; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; SSF47928; 1. DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00673570}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01416}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00673590}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00673577}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00673593}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01416, KW ECO:0000256|SAAS:SAAS00673594}. SQ SEQUENCE 177 AA; 19412 MW; 93DE29EFD9D9EF13 CRC64; MSEFVTVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG ALAPETLAES FIAVCGEQLD ENGQNLIRVM AENNRLNALP DVLEQFIHLR AASEATSEVE VTSATALSEE QLSKISAAME KRLSRKVKLN CKIDKSVMAG VIIRAGDMVI DGSVRGRLER LADVLQS //