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ATPD_ENTHA
ID   ATPD_ENTHA              Reviewed;         180 AA.
AC   P26680; I6SYU5;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE   AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE   AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE            Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN   Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; OrderedLocusNames=EHR_08485;
OS   Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS   NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=768486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC   / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX   PubMed=1328152; DOI=10.1128/jb.174.19.6117-6124.1992;
RA   Shibata C., Ehara T., Tomura K., Igarashi K., Kobayashi H.;
RT   "Gene structure of Enterococcus hirae (Streptococcus faecalis) F1F0-ATPase,
RT   which functions as a regulator of cytoplasmic pH.";
RL   J. Bacteriol. 174:6117-6124(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC   / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX   PubMed=22933757; DOI=10.1128/jb.01075-12;
RA   Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT   "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT   a model organism for the study of ion transport, bioenergetics, and copper
RT   homeostasis.";
RL   J. Bacteriol. 194:5126-5127(2012).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01416};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR   EMBL; M64265; AAA26863.1; -; Genomic_DNA.
DR   EMBL; M90060; AAA26856.1; -; Genomic_DNA.
DR   EMBL; CP003504; AFM70622.1; -; Genomic_DNA.
DR   PIR; E43259; E43259.
DR   RefSeq; WP_010737988.1; NZ_KB946231.1.
DR   AlphaFoldDB; P26680; -.
DR   SMR; P26680; -.
DR   STRING; 768486.EHR_08485; -.
DR   EnsemblBacteria; AFM70622; AFM70622; EHR_08485.
DR   KEGG; ehr:EHR_08485; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_4_1_9; -.
DR   OrthoDB; 1937493at2; -.
DR   Proteomes; UP000002895; 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; -; 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; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Transport.
FT   CHAIN           1..180
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000193464"
SQ   SEQUENCE   180 AA;  20698 MW;  202A2F744594161E CRC64;
     MKLDKYTVGR RYGKALFELA IDSNSAEEIY QELLSLRQIY SEIPGLGNVL SDVRLEPHEK
     RIIMDKLVSG FDGIVKNFLE VVYSYNRMSE LSFMIDEYEH RYNDYKGLLL GSVKTAVPLS
     DEQLQKLEMN VAKTMDYQTV ELKQIVDSSI IGGAIVEANH RVIDGSIRTQ LEKMRNQLNR
 
 
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