FRDC_ESCF3
ID FRDC_ESCF3 Reviewed; 131 AA.
AC B7LLT6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=EFER_4206;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ91626.1; -; Genomic_DNA.
DR RefSeq; WP_000208757.1; NC_011740.1.
DR AlphaFoldDB; B7LLT6; -.
DR SMR; B7LLT6; -.
DR EnsemblBacteria; CAQ91626; CAQ91626; EFER_4206.
DR GeneID; 66671934; -.
DR KEGG; efe:EFER_4206; -.
DR HOGENOM; CLU_156492_0_0_6; -.
DR OMA; MTATWWQ; -.
DR OrthoDB; 2053102at2; -.
DR BioCyc; EFER585054:EFER_RS20980-MON; -.
DR Proteomes; UP000000745; 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..131
FT /note="Fumarate reductase subunit C"
FT /id="PRO_1000132377"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT TRANSMEM 63..83
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; 15015 MW; 26FDF83A2EF8EF43 CRC64;
MTTKRKPYVR PMTSTWWKKL PFYRFYMLRE GTAVPAVWFS IELIFGLFAL KNGPEAWAGF
VDFLQNPVIV IINLITLAAA LLHTKTWFEL APKAANIIVK DEKMGPEPII KSLWAVTVVA
TIVILFVALY W