ID   FRDC_YERE8              Reviewed;         130 AA.
AC   A1JIQ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Fumarate reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00708};
DE   AltName: Full=Fumarate reductase 15 kDa hydrophobic protein {ECO:0000255|HAMAP-Rule:MF_00708};
DE   AltName: Full=Quinol-fumarate reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00708};
DE            Short=QFR subunit C {ECO:0000255|HAMAP-Rule:MF_00708};
GN   Name=frdC {ECO:0000255|HAMAP-Rule:MF_00708}; OrderedLocusNames=YE0362;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are
CC       responsible for the catalysis of fumarate and succinate
CC       interconversion; fumarate reductase is used in anaerobic growth, and
CC       succinate dehydrogenase is used in aerobic growth. Anchors the
CC       catalytic components of the fumarate reductase complex to the cell
CC       inner membrane, binds quinones. {ECO:0000255|HAMAP-Rule:MF_00708}.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic
CC       anchor proteins (FrdC and FrdD). {ECO:0000255|HAMAP-Rule:MF_00708}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00708}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00708}.
CC   -!- SIMILARITY: Belongs to the FrdC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00708}.
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DR   EMBL; AM286415; CAL10492.1; -; Genomic_DNA.
DR   RefSeq; WP_005175556.1; NC_008800.1.
DR   RefSeq; YP_001004738.1; NC_008800.1.
DR   AlphaFoldDB; A1JIQ1; -.
DR   SMR; A1JIQ1; -.
DR   STRING; 393305.YE0362; -.
DR   EnsemblBacteria; CAL10492; CAL10492; YE0362.
DR   KEGG; yen:YE0362; -.
DR   PATRIC; fig|393305.7.peg.459; -.
DR   eggNOG; COG3029; Bacteria.
DR   HOGENOM; CLU_156492_0_0_6; -.
DR   OMA; MTATWWQ; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045284; C:plasma membrane fumarate reductase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00546; QFR_TypeD_subunitC; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   HAMAP; MF_00708; Fumarate_red_C; 1.
DR   InterPro; IPR003510; Fumarate_red_C.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   Pfam; PF02300; Fumarate_red_C; 1.
DR   PIRSF; PIRSF000180; FrdC; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..130
FT                   /note="Fumarate reductase subunit C"
FT                   /id="PRO_1000045538"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
SQ   SEQUENCE   130 AA;  14593 MW;  9BB3AA108B8DDA89 CRC64;
     MTTKRKAYVR TMAPNWWQQL GFYRFYMLRE GTSVPTVWFS ILLIYGVFAL KSGPAGWEGF
     VGFLQNPLVL LINIITLLAA VLHTKTWFEL APKAANIIVK DEKMGPEPVI KALWVVTIVA
     TAIILAVALL