ID   ATPL_WOLPP              Reviewed;          75 AA.
AC   B3CLG2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE            Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; OrderedLocusNames=WP0622;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(2008).
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_01396}.
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. {ECO:0000255|HAMAP-Rule:MF_01396}.
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_01396}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01396};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01396}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
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DR   EMBL; AM999887; CAQ54730.1; -; Genomic_DNA.
DR   RefSeq; WP_006014985.1; NC_010981.1.
DR   AlphaFoldDB; B3CLG2; -.
DR   SMR; B3CLG2; -.
DR   STRING; 570417.WP0622; -.
DR   EnsemblBacteria; CAQ54730; CAQ54730; WP0622.
DR   GeneID; 61803032; -.
DR   KEGG; wpi:WP0622; -.
DR   eggNOG; COG0636; Bacteria.
DR   HOGENOM; CLU_148047_4_0_5; -.
DR   OMA; CMGFCIL; -.
DR   OrthoDB; 2078221at2; -.
DR   Proteomes; UP000008814; Chromosome.
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; IPR005953; ATP_synth_csu_bac/chlpt.
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   PANTHER; PTHR10031; PTHR10031; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
DR   TIGRFAMs; TIGR01260; ATP_synt_c; 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..75
FT                   /note="ATP synthase subunit c"
FT                   /id="PRO_1000184535"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT   SITE            58
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ   SEQUENCE   75 AA;  7826 MW;  72ECFB9AC769F68E CRC64;
     MDLVALKFIA IGLAVFGMLG AGLGIANIFS AMLNGIARNP ESEGKMKSYV YIGAAMVEIM
     GLLAFVLAML LIFAA