ID A0A1W1YC66_9PSED Unreviewed; 178 AA. AC A0A1W1YC66; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 19-JAN-2022, entry version 16. 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=SAMN05660385_00131 {ECO:0000313|EMBL:SMC33762.1}; OS Pseudomonas sp. URIL14HWK12:I5. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1261630 {ECO:0000313|EMBL:SMC33762.1, ECO:0000313|Proteomes:UP000192695}; RN [1] {ECO:0000313|EMBL:SMC33762.1, ECO:0000313|Proteomes:UP000192695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=URIL14HWK12:I5 {ECO:0000313|EMBL:SMC33762.1, RC ECO:0000313|Proteomes:UP000192695}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-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 --------------------------------------------------------------------------- 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; FWXQ01000001; SMC33762.1; -; Genomic_DNA. DR RefSeq; WP_003253191.1; NZ_FWXQ01000001.1. DR SMR; A0A1W1YC66; -. DR EnsemblBacteria; SMC33762; SMC33762; SAMN05660385_00131. DR GeneID; 61771164; -. DR GeneID; 66675396; -. DR Proteomes; UP000192695; 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; PTHR11910; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; SSF47928; 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 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}. SQ SEQUENCE 178 AA; 19197 MW; D39FC622311FA327 CRC64; MAELTTLARP YAKAAFEHAQ AHQQLANWSA MLGLAAAVSQ DDTMQRLLKA PRLTSAEKAA TFIDVCGDKF NAQAQNFIHV AAENDRLLLL PEIAALFDLY KAEQEKSVDV EVTSAFALNQ EQQDKLAKVL SARLGQEVRL HASEDASLIG GVVIRAGDLV IDGSVRGKIA KLAEALKS //