ID   ATPD_LACAC              Reviewed;         182 AA.
AC   Q9RGY4; Q5FKY3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=LBA0775;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, INDUCTION, AND
RP   PROBABLE OPERON.
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=10510230; DOI=10.1046/j.1365-2958.1999.01557.x;
RA   Kullen M.J., Klaenhammer T.R.;
RT   "Identification of the pH-inducible, proton-translocating F1F0-ATPase
RT   (atpBEFHAGDC) operon of Lactobacillus acidophilus by differential display:
RT   gene structure, cloning and characterization.";
RL   Mol. Microbiol. 33:1152-1161(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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   -!- ACTIVITY REGULATION: Increases 2-fold following exposure to low pH.
CC       {ECO:0000269|PubMed:10510230}.
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   -!- INDUCTION: By low pH. {ECO:0000269|PubMed:10510230}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|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; AF098522; AAF22495.1; -; Genomic_DNA.
DR   EMBL; CP000033; AAV42641.1; -; Genomic_DNA.
DR   RefSeq; WP_003546742.1; NC_006814.3.
DR   RefSeq; YP_193672.1; NC_006814.3.
DR   AlphaFoldDB; Q9RGY4; -.
DR   SMR; Q9RGY4; -.
DR   STRING; 272621.LBA0775; -.
DR   PRIDE; Q9RGY4; -.
DR   EnsemblBacteria; AAV42641; AAV42641; LBA0775.
DR   GeneID; 56942402; -.
DR   KEGG; lac:LBA0775; -.
DR   PATRIC; fig|272621.13.peg.737; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_4_1_9; -.
DR   OMA; MVDNIQD; -.
DR   BioCyc; LACI272621:G1G49-791-MON; -.
DR   Proteomes; UP000006381; 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   2: Evidence at transcript level;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..182
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000371007"
SQ   SEQUENCE   182 AA;  20338 MW;  27945E10EFBDC4F9 CRC64;
     MALSREEVAA RYGTALFGYA QDNKVLDTVY DEMMALKKAA IANPKFISVL SDPILSSKDK
     KSILTAVEKD FSDEVQGFLN LLLEYNRFAD LIDIIDQFSL LYDNENKIAS GTATTAVKLD
     DDQLERLSES FAKKYDLNAV RLENKVDPSI LGGVILQVKD RVIDGSVKNK LKKIRAQIID
     EN