ID   FRDC_ALISL              Reviewed;         127 AA.
AC   B6EMS0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Fumarate reductase subunit C {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=VSAL_I2790;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- FUNCTION: Anchors the catalytic components of the fumarate reductase
CC       complex to the cell membrane, binds quinones. {ECO:0000255|HAMAP-
CC       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; FM178379; CAQ80474.1; -; Genomic_DNA.
DR   RefSeq; WP_012551226.1; NC_011312.1.
DR   AlphaFoldDB; B6EMS0; -.
DR   SMR; B6EMS0; -.
DR   STRING; 316275.VSAL_I2790; -.
DR   EnsemblBacteria; CAQ80474; CAQ80474; VSAL_I2790.
DR   KEGG; vsa:VSAL_I2790; -.
DR   eggNOG; COG3029; Bacteria.
DR   HOGENOM; CLU_156492_0_0_6; -.
DR   OMA; MTATWWQ; -.
DR   OrthoDB; 2053102at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
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..127
FT                   /note="Fumarate reductase subunit C"
FT                   /id="PRO_1000132368"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
SQ   SEQUENCE   127 AA;  14353 MW;  2F694578C2A94900 CRC64;
     MSNRKPYVRE MTRTWWKDHP FYRFYMVREA TILPLIFFTI CLLVGLGSLV KGPLAWASWL
     DFMANPIVVA LNIVALAGSL FHAQTFFSMM PQVMPIRLGG KTLDKKVVVL AQWAAVAAIT
     LLVLVIV