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FRDC_SHIDS
ID   FRDC_SHIDS              Reviewed;         131 AA.
AC   Q328H2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
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}; OrderedLocusNames=SDY_4396;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB64283.1; -; Genomic_DNA.
DR   RefSeq; WP_000208755.1; NC_007606.1.
DR   RefSeq; YP_405774.1; NC_007606.1.
DR   AlphaFoldDB; Q328H2; -.
DR   SMR; Q328H2; -.
DR   STRING; 300267.SDY_4396; -.
DR   EnsemblBacteria; ABB64283; ABB64283; SDY_4396.
DR   KEGG; sdy:SDY_4396; -.
DR   PATRIC; fig|300267.13.peg.5192; -.
DR   HOGENOM; CLU_156492_0_0_6; -.
DR   OMA; MTATWWQ; -.
DR   Proteomes; UP000002716; 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_1000045533"
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;  14997 MW;  26FDF83E6EBCEF43 CRC64;
     MTTKRKPYVR PMTSTWWKKL PFYRFYMLRE GTAVPAVWFS IELIFGLFAL KNGPEAWAGF
     VDFLQNPVIV IINLITLAAA LLHTKTWFEL APKAANIIVK DEKIGPEPII KSLWAVTVVA
     TIVILFVALY W
 
 
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