ID   ATPL_STROR              Reviewed;          66 AA.
AC   P50017;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=ATP synthase subunit c;
DE   AltName: Full=ATP synthase F(0) sector subunit c;
DE   AltName: Full=F-type ATPase subunit c;
DE            Short=F-ATPase subunit c;
DE   AltName: Full=Lipid-binding protein;
GN   Name=atpE; Synonyms=atpC;
OS   Streptococcus oralis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35037 / CIP 102922 / DSM 20627 / KCTC 13048 / LMG 14532 / NCTC
RC   11427 / PB182, and M222;
RX   PubMed=7934882; DOI=10.1111/j.1365-2958.1994.tb01045.x;
RA   Fenoll A., Munoz R., Garcia E., de la Campa A.G.;
RT   "Molecular basis of the optochin-sensitive phenotype of pneumococcus:
RT   characterization of the genes encoding the F0 complex of the Streptococcus
RT   pneumoniae and Streptococcus oralis H(+)-ATPases.";
RL   Mol. Microbiol. 12:587-598(1994).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC       translocation across the membrane. A homomeric c-ring of between 10-14
CC       subunits forms the central stalk rotor element with the F(1) delta and
CC       epsilon subunits (By similarity). {ECO:0000250}.
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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: M222 is an optochin-resistant (OptR) strain produced by
CC       interspecies recombination between S.pneumoniae and S.oralis.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; Z26850; CAA81447.1; -; Genomic_DNA.
DR   EMBL; Z26852; CAA81455.1; -; Genomic_DNA.
DR   PIR; S49407; S49407.
DR   RefSeq; WP_001054556.1; NZ_RMVL01000001.1.
DR   AlphaFoldDB; P50017; -.
DR   SMR; P50017; -.
DR   STRING; 1303.SORDD17_01210; -.
DR   GeneID; 49599621; -.
DR   OMA; MNLTFFG; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.20.10; -; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Lipid-binding; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..66
FT                   /note="ATP synthase subunit c"
FT                   /id="PRO_0000112168"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            52
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   66 AA;  7219 MW;  611FFBECF6639D07 CRC64;
     MNLTFFGLCL ACMGVSLAEG MLMNGLFKSA ARQPDIIPQL RSLMIMGIAF IEGTFLVTLV
     FSFVIK