ID A0A0K1JLB1_9MICO Unreviewed; 270 AA.
AC A0A0K1JLB1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=VV02_19480 {ECO:0000313|EMBL:AKU17514.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU17514.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU17514.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU17514.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) 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}.
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DR EMBL; CP011112; AKU17514.1; -; Genomic_DNA.
DR RefSeq; WP_052594213.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JLB1; -.
DR STRING; 571913.VV02_19480; -.
DR KEGG; lmoi:VV02_19480; -.
DR PATRIC; fig|571913.6.peg.3944; -.
DR OrthoDB; 5242917at2; -.
DR Proteomes; UP000066480; Chromosome.
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 HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
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 PROSITE; PS00389; ATPASE_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|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 Reference proteome {ECO:0000313|Proteomes:UP000066480};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ SEQUENCE 270 AA; 29026 MW; B6CC234C16BEBF46 CRC64;
MQGASRSALA KGRDELGQIL ASVIDSTQIG DELFFAGQTL DGSASLRRAL ADPSREAAPK
QDLVERLFGG KVGNETLELL RALVAQRWSG ERDLADALDL LGAEAIVASA EQQGRLDQVE
DDLFRYGRTV AGDAGLRDAY NDRQRSGADK ATLTTRLLDG KAAPESVRLA AHAAEAPRGR
RFEKALEGYV AVATQRREQL TALVTAAVPL DPTHVQRLKQ ALNDMYGKPV QVNVVLDPHV
VGGLRVQIGD EVIDGTIARR LDDARRGLAS
//