ID   FRDC_PROVU              Reviewed;         131 AA.
AC   P20923;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 80.
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};
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3308458; DOI=10.1111/j.1432-1033.1987.tb13362.x;
RA   Cole S.T.;
RT   "Nucleotide sequence and comparative analysis of the frd operon encoding
RT   the fumarate reductase of Proteus vulgaris. Extensive sequence divergence
RT   of the membrane anchors and absence of an frd-linked ampC cephalosporinase
RT   gene.";
RL   Eur. J. Biochem. 167:481-488(1987).
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, ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00708}.
CC   -!- SIMILARITY: Belongs to the FrdC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00708}.
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DR   EMBL; X06144; CAA29503.1; -; Genomic_DNA.
DR   PIR; S00109; RDEB15.
DR   AlphaFoldDB; P20923; -.
DR   SMR; P20923; -.
DR   STRING; 585.DR95_2060; -.
DR   eggNOG; COG3029; Bacteria.
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..131
FT                   /note="Fumarate reductase subunit C"
FT                   /id="PRO_0000196533"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT   TRANSMEM        58..78
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   131 AA;  14836 MW;  DB4313F3753853F9 CRC64;
     MTTKRKPYVR GMQPNWWTKL GFYRFYITRE GTCLPQLWFS LVVLFGVFAL KNGPESWAGF
     VGFLSNPILM LINIVTLIAT VFHTATWFKL APKAVNIVVK DEKLPQEPIV RGLWGLTIVV
     TVVILAVALI V