FRDC_YERPG
ID FRDC_YERPG Reviewed; 130 AA.
AC A9QYP6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=YpAngola_A0716;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX88314.1; -; Genomic_DNA.
DR RefSeq; WP_012229099.1; NZ_CP009935.1.
DR AlphaFoldDB; A9QYP6; -.
DR SMR; A9QYP6; -.
DR KEGG; ypg:YpAngola_A0716; -.
DR PATRIC; fig|349746.12.peg.1663; -.
DR OMA; MTATWWQ; -.
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..130
FT /note="Fumarate reductase subunit C"
FT /id="PRO_1000132391"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00708"
SQ SEQUENCE 130 AA; 14695 MW; CFFD0FF58AC7588E CRC64;
MTTKRKAYVR TMAPNWWQQL GFYRFYMLRE GTSIPAVWFS VLLIYGVFSL KSGPAGWEGF
VSFLQNPLVL FLNILTLFAA LLHTKTWFEL APKAVNIIVK SEKMGPEPMI KALWVVTVVA
SAIILAVALL
