ID A0A2D7NRF6_9DELT Unreviewed; 183 AA. AC A0A2D7NRF6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 14-DEC-2022, entry version 11. 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 ECO:0000313|EMBL:MAJ49500.1}; GN ORFNames=CL937_07325 {ECO:0000313|EMBL:MAJ49500.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ49500.1, ECO:0000313|Proteomes:UP000226880}; RN [1] {ECO:0000313|Proteomes:UP000226880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_01416}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01416}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000256|HAMAP-Rule:MF_01416}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MAJ49500.1}. 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; NZHX01000109; MAJ49500.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2D7NRF6; -. DR Proteomes; UP000226880; Unassembled WGS sequence. 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; -; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 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 TIGRFAMs; TIGR01145; ATP_synt_delta; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01416}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01416}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01416}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01416}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01416}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}. FT COILED 7..37 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 183 AA; 20213 MW; E6FF75AE131A5CC9 CRC64; MSQGIVAQRY AKALIGLTKT RKELEEAGEK LSEASEAYQS SVELQEILAS NKVSYPVKQK ILGELLERLK TSTLIHTFCR YLLSKRRFEL IPSISKAYDQ MFQAKIGRVE AQVSVTHELS DASRKKLEKT LSSLTGKEVQ VSVNIDSGLI GGIVTRIGST VYDGSLRNQL NLIHQSISKG GTL //