FRDC_SHIFL
ID FRDC_SHIFL Reviewed; 131 AA.
AC Q83P38;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
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};
GN OrderedLocusNames=SF4310, S4575;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN45728.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19512.1; -; Genomic_DNA.
DR RefSeq; NP_710021.1; NC_004337.2.
DR RefSeq; WP_000208747.1; NZ_WPGW01000002.1.
DR AlphaFoldDB; Q83P38; -.
DR SMR; Q83P38; -.
DR STRING; 198214.SF4310; -.
DR EnsemblBacteria; AAN45728; AAN45728; SF4310.
DR EnsemblBacteria; AAP19512; AAP19512; S4575.
DR GeneID; 1026766; -.
DR KEGG; sfl:SF4310; -.
DR KEGG; sfx:S4575; -.
DR PATRIC; fig|198214.7.peg.5081; -.
DR HOGENOM; CLU_156492_0_0_6; -.
DR OMA; MTATWWQ; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..131
FT /note="Fumarate reductase subunit C"
FT /id="PRO_0000196536"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT TRANSMEM 57..77
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; 15059 MW; 038EFE5C2EE680B8 CRC64;
MTTKRKPYVR PMTSTWWKKL PFYRFYMLRE GTAVPAVWFS IELIFALFAL KNGPEAWAGF
VDFLQNPVIV IINLITLTAA LLHTKTWFEL APKAANIIVK DEKMGPEPII KSLWAVTVVA
TIVILFVALY W
