ID   ATPD_LEUMM              Reviewed;         180 AA.
AC   Q03V26;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=LEUM_1872;
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS   20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS   8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC   / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000414; ABJ62946.1; -; Genomic_DNA.
DR   RefSeq; WP_011680435.1; NC_008531.1.
DR   AlphaFoldDB; Q03V26; -.
DR   SMR; Q03V26; -.
DR   STRING; 203120.LEUM_1872; -.
DR   EnsemblBacteria; ABJ62946; ABJ62946; LEUM_1872.
DR   GeneID; 61177714; -.
DR   KEGG; lme:LEUM_1872; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_4_1_9; -.
DR   OMA; MVDNIQD; -.
DR   OrthoDB; 1937493at2; -.
DR   Proteomes; UP000000362; 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; 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; 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_1000184746"
SQ   SEQUENCE   180 AA;  19392 MW;  3E8F4EC3A1FF2311 CRC64;
     MAKNIKDIAN QYAKAIFELA GEQDNVDEVL TDLRTIKTVL DENQNFITIA SSADVAIASR
     DDLLKTLTGN STDSVKNLVK LLQVNNRLNI LSIVVDEFVS QYNEVNGIVD VQATTAVALD
     DGRLDKLASV FASKTGAQQV NIENVVDESI LGGVILQSQS TLIDGSLQTK IAKMKAQLLG