ID   ATPD_STRMU              Reviewed;         178 AA.
AC   P95786;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 134.
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}; Synonyms=atpE;
GN   OrderedLocusNames=SMU_1531;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=8996091; DOI=10.1016/s0378-1119(96)00502-1;
RA   Smith A.J., Quivey R.G., Faustoferri R.C.;
RT   "Cloning and nucleotide sequence analysis of the Streptococcus mutans
RT   membrane-bound, proton-translocating ATPase operon.";
RL   Gene 183:87-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; U31170; AAD13380.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59181.1; -; Genomic_DNA.
DR   PIR; JC5738; JC5738.
DR   RefSeq; NP_721875.1; NC_004350.2.
DR   RefSeq; WP_002262943.1; NC_004350.2.
DR   AlphaFoldDB; P95786; -.
DR   SMR; P95786; -.
DR   STRING; 210007.SMU_1531; -.
DR   PRIDE; P95786; -.
DR   EnsemblBacteria; AAN59181; AAN59181; SMU_1531.
DR   KEGG; smu:SMU_1531; -.
DR   PATRIC; fig|210007.7.peg.1363; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_1_2_9; -.
DR   OMA; QVIVAHE; -.
DR   PhylomeDB; P95786; -.
DR   SABIO-RK; P95786; -.
DR   Proteomes; UP000002512; 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; Reference proteome; Transport.
FT   CHAIN           1..178
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000193490"
FT   CONFLICT        60
FT                   /note="S -> A (in Ref. 1; AAD13380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="Missing (in Ref. 1; AAD13380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  20449 MW;  FFE8F6F17D1ECCF8 CRC64;
     MDKKTQAVTE IYAKSLVEVA LERDSVPIIY DEVRAILSVL DDQQVQDFLA SKAIDLSAKS
     EVVRLFQESC SNYMKQFLEI ILQNERQQLL YLIMKEVLKE LSLKTHIFDI EVTTAVALSD
     DQKERLTALV EKKFALTKRN LIEKIDDEII GGFIIKANNK VIDTSIRSQL QELKMNLK