ID A0A3A3JZ35_SALMO Unreviewed; 177 AA. AC A0A3A3JZ35; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 31-JUL-2019, entry version 6. 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=AAN00_21440 {ECO:0000313|EMBL:EAB5750073.1}, AXU21_21590 GN {ECO:0000313|EMBL:EAA9236925.1}, AXU38_19685 GN {ECO:0000313|EMBL:EAA5756226.1}, CM22_22220 GN {ECO:0000313|EMBL:EAA7521920.1}, CVB19_15680 GN {ECO:0000313|EMBL:EAA8535367.1}, QB52_20670 GN {ECO:0000313|EMBL:EAA7133640.1}, UK00_19545 GN {ECO:0000313|EMBL:EAA8125053.1}, XU87_21565 GN {ECO:0000313|EMBL:EAA9555910.1}; OS Salmonella montevideo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=115981 {ECO:0000313|EMBL:EAA9555910.1}; RN [1] {ECO:0000313|EMBL:EAA7133640.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=64947 {ECO:0000313|EMBL:EAB5750073.1}, and H120360356 RC {ECO:0000313|EMBL:EAA7133640.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAA9555910.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ADRDL-1578 {ECO:0000313|EMBL:EAA8535367.1}, CFSAN004243 RC {ECO:0000313|EMBL:EAA8125053.1}, CFSAN032150 RC {ECO:0000313|EMBL:EAA9236925.1}, CFSAN032167 RC {ECO:0000313|EMBL:EAA5756226.1}, MDH-2014-00193 RC {ECO:0000313|EMBL:EAA7521920.1}, and NY-N13154 RC {ECO:0000313|EMBL:EAA9555910.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUL-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:EAA9555910.1}. 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; AAABXU010000016; EAA5756226.1; -; Genomic_DNA. DR EMBL; AAACJZ010000025; EAA7133640.1; -; Genomic_DNA. DR EMBL; AAACMB010000016; EAA7521920.1; -; Genomic_DNA. DR EMBL; AAACQX010000017; EAA8125053.1; -; Genomic_DNA. DR EMBL; AAACTW010000033; EAA8535367.1; -; Genomic_DNA. DR EMBL; AAACZB010000017; EAA9236925.1; -; Genomic_DNA. DR EMBL; AAADCM010000018; EAA9555910.1; -; Genomic_DNA. DR EMBL; AAAFDE010000023; EAB5750073.1; -; Genomic_DNA. DR RefSeq; WP_001288957.1; NZ_UGXO01000003.1. DR EnsemblBacteria; AKH09502; AKH09502; SE14_04103. DR EnsemblBacteria; OCS93583; OCS93583; A7B05_23755. DR EnsemblBacteria; OCT01184; OCT01184; A7B04_06045. 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule. 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 //