ID   VATC_METBU              Reviewed;         357 AA.
AC   Q12WL3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=V-type ATP synthase subunit C {ECO:0000255|HAMAP-Rule:MF_00314};
DE   AltName: Full=V-ATPase subunit C {ECO:0000255|HAMAP-Rule:MF_00314};
GN   Name=atpC {ECO:0000255|HAMAP-Rule:MF_00314}; OrderedLocusNames=Mbur_1241;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00314}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00314}.
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DR   EMBL; CP000300; ABE52163.1; -; Genomic_DNA.
DR   RefSeq; WP_011499309.1; NC_007955.1.
DR   AlphaFoldDB; Q12WL3; -.
DR   SMR; Q12WL3; -.
DR   STRING; 259564.Mbur_1241; -.
DR   PRIDE; Q12WL3; -.
DR   EnsemblBacteria; ABE52163; ABE52163; Mbur_1241.
DR   GeneID; 3998565; -.
DR   KEGG; mbu:Mbur_1241; -.
DR   HOGENOM; CLU_059311_0_1_2; -.
DR   OMA; LRKFDVW; -.
DR   OrthoDB; 75042at2157; -.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   HAMAP; MF_00314; ATP_synth_C_arch; 1.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR014272; ATPase_V0-cplx_c_su.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
DR   TIGRFAMs; TIGR02923; AhaC; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..357
FT                   /note="V-type ATP synthase subunit C"
FT                   /id="PRO_1000048370"
SQ   SEQUENCE   357 AA;  40934 MW;  D1B098649F94D84B CRC64;
     MRLLQKFTRK SSLKQSGSSS NYAYVTARVR AMKSNLLPRE VYPRLMNMGI DEITRFIEES
     QYKQDVDELA RTYDGVDLFE HALNRNLAVT FTKLINISEG ELNYLISEYL RKYDIWSIKT
     ILRGKYCGAS VEEINDSIVS AGQLSYPFLL SLSEKESYES IIDALSGTDY YPTLKEYDGT
     NLSDIENKLD KMYYTGLSTT VNNPKSNDSK LFSKFIRTEI DIKNLSTLFR LKNAGVEKDE
     IADLILEGGL HLSIKEIEKL LPLPFSEFVQ SLEKYPYWED ISGIVKTEMD SLIELETQLT
     RSNIKSASSF SHVYPLSIVP IMDYILNKTN EVHNLRIILR GKAANLDEEI IRNQLVI