ID   ATPD_LACGA              Reviewed;         182 AA.
AC   Q042L2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=LGAS_1241;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS   102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC   3163 / NCIMB 11718 / NCTC 13722 / AM63;
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; CP000413; ABJ60610.1; -; Genomic_DNA.
DR   RefSeq; WP_003647069.1; NZ_WBMG01000002.1.
DR   AlphaFoldDB; Q042L2; -.
DR   SMR; Q042L2; -.
DR   GeneID; 66469257; -.
DR   KEGG; lga:LGAS_1241; -.
DR   HOGENOM; CLU_085114_4_1_9; -.
DR   OMA; MVDNIQD; -.
DR   OrthoDB; 1937493at2; -.
DR   BioCyc; LGAS324831:G1G6Y-1237-MON; -.
DR   Proteomes; UP000000664; 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..182
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_1000184735"
SQ   SEQUENCE   182 AA;  20760 MW;  D43E6727EC890070 CRC64;
     MALSREEIAS RYSKALFAYA QDAKKLDEVH EDMNVLLQVA KENPDMLRLL SDPIIRKNQK
     EEFLSSFSGE FSSETKNFLE FLLEYGRFNA LTEIIKAFDA LYDEDKNIAS GTAVSAINLD
     EDELNRISQA YAKKYGFKKL ILTNEVDSSI LGGIILKVGD RIIDGSIRTR LQQIREQLIE
     NR