ID L0EI07_THECK Unreviewed; 179 AA.
AC L0EI07;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 OrderedLocusNames=Theco_3862 {ECO:0000313|EMBL:AGA59873.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA59873.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) 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 -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000256|HAMAP-Rule:MF_01416}.
CC -!- SUBCELLULAR LOCATION: Cell inner 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}.
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DR EMBL; CP003255; AGA59873.1; -; Genomic_DNA.
DR RefSeq; WP_015256588.1; NC_019897.1.
DR AlphaFoldDB; L0EI07; -.
DR STRING; 717605.Theco_3862; -.
DR KEGG; tco:Theco_3862; -.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_085114_1_1_9; -.
DR OMA; MVDNIQD; -.
DR OrthoDB; 9802471at2; -.
DR Proteomes; UP000010795; 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 Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 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 NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR PANTHER; PTHR11910:SF22; ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC; 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.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01416}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW 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:UP000010795};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ SEQUENCE 179 AA; 19352 MW; DBD1D7069A70E1EE CRC64;
MSADSVAAKR YAKALYEAAA QQDLVWDVEQ QLKALVDALE QTPEFKAFLG SPNIETSRKI
SVLEEALAGK TSDLLTRFIR LLIERGRQAD LPGVYRAYAR IAGDASGQAR AIVYTAKPLG
EAELAAIAEQ FGKVTGKTIR AEQEVDPSLI GGVMVRIGDR LYDGSLSGKL ARLEKALIS
//