FRDC_ECOLI
ID FRDC_ECOLI Reviewed; 131 AA.
AC P0A8Q0; P03805; Q2M6F0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 128.
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, ECO:0000303|PubMed:11850430};
DE Short=QFR subunit C {ECO:0000255|HAMAP-Rule:MF_00708, ECO:0000303|PubMed:11850430};
GN Name=frdC {ECO:0000255|HAMAP-Rule:MF_00708};
GN OrderedLocusNames=b4152, JW4113;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7041115; DOI=10.1073/pnas.79.4.1111;
RA Grundstroem T., Jaurin B.;
RT "Overlap between ampC and frd operons on the Escherichia coli chromosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH MENAQUINONE,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10373108; DOI=10.1126/science.284.5422.1961;
RA Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C.;
RT "Structure of the Escherichia coli fumarate reductase respiratory
RT complex.";
RL Science 284:1961-1966(1999).
RN [7] {ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, ECO:0007744|PDB:1L0V}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-131 IN COMPLEX WITH MENAQUINONE
RP AND INHIBITORS, AND SUBUNIT.
RX PubMed=11850430; DOI=10.1074/jbc.m200815200;
RA Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C.;
RT "Crystallographic studies of the Escherichia coli quinol-fumarate reductase
RT with inhibitors bound to the quinol-binding site.";
RL J. Biol. Chem. 277:16124-16130(2002).
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 (PubMed:10373108). The QFR enzyme
CC complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S]
CC cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic
CC side of the membrane) while QD (the distal cluster) is on the other
CC side of the membrane. It is not clear if both of the quinol-binding
CC sites are functionally relevant (PubMed:10373108, PubMed:11850430).
CC {ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:11850430}.
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 ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:11850430}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00708, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00708, ECO:0000269|PubMed:10373108}.
CC -!- SIMILARITY: Belongs to the FrdC family. {ECO:0000255|HAMAP-
CC Rule:MF_00708}.
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DR EMBL; J01611; AAA23439.1; -; Genomic_DNA.
DR EMBL; V00277; CAA23535.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97051.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77112.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78156.1; -; Genomic_DNA.
DR PIR; S56380; S56380.
DR RefSeq; NP_418576.1; NC_000913.3.
DR RefSeq; WP_000208757.1; NZ_SSZK01000018.1.
DR PDB; 1KF6; X-ray; 2.70 A; C/O=2-131.
DR PDB; 1KFY; X-ray; 3.60 A; C/O=2-131.
DR PDB; 1L0V; X-ray; 3.30 A; C/O=2-131.
DR PDB; 2B76; X-ray; 3.30 A; C/O=2-131.
DR PDB; 3CIR; X-ray; 3.65 A; C/O=2-131.
DR PDB; 3P4P; X-ray; 2.80 A; C/O=2-131.
DR PDB; 3P4Q; X-ray; 3.35 A; C/O=2-131.
DR PDB; 3P4R; X-ray; 3.05 A; C/O=2-131.
DR PDB; 3P4S; X-ray; 3.10 A; C/O=2-131.
DR PDB; 5VPN; X-ray; 4.22 A; C/G=2-131.
DR PDBsum; 1KF6; -.
DR PDBsum; 1KFY; -.
DR PDBsum; 1L0V; -.
DR PDBsum; 2B76; -.
DR PDBsum; 3CIR; -.
DR PDBsum; 3P4P; -.
DR PDBsum; 3P4Q; -.
DR PDBsum; 3P4R; -.
DR PDBsum; 3P4S; -.
DR PDBsum; 5VPN; -.
DR AlphaFoldDB; P0A8Q0; -.
DR SMR; P0A8Q0; -.
DR BioGRID; 4262700; 364.
DR ComplexPortal; CPX-1967; Plasma membrane fumarate reductase complex.
DR DIP; DIP-48082N; -.
DR IntAct; P0A8Q0; 3.
DR STRING; 511145.b4152; -.
DR DrugBank; DB07490; 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL.
DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide.
DR jPOST; P0A8Q0; -.
DR PaxDb; P0A8Q0; -.
DR PRIDE; P0A8Q0; -.
DR EnsemblBacteria; AAC77112; AAC77112; b4152.
DR EnsemblBacteria; BAE78156; BAE78156; BAE78156.
DR GeneID; 66671934; -.
DR GeneID; 948680; -.
DR KEGG; ecj:JW4113; -.
DR KEGG; eco:b4152; -.
DR PATRIC; fig|1411691.4.peg.2546; -.
DR EchoBASE; EB0328; -.
DR eggNOG; COG3029; Bacteria.
DR HOGENOM; CLU_156492_0_0_6; -.
DR InParanoid; P0A8Q0; -.
DR OMA; MTATWWQ; -.
DR PhylomeDB; P0A8Q0; -.
DR BioCyc; EcoCyc:FUM-MEMB1; -.
DR BioCyc; MetaCyc:FUM-MEMB1; -.
DR BRENDA; 1.3.5.4; 2026.
DR EvolutionaryTrace; P0A8Q0; -.
DR PRO; PR:P0A8Q0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0045284; C:plasma membrane fumarate reductase complex; IDA:EcoCyc.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IMP:EcoCyc.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:EcoCyc.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0006113; P:fermentation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..131
FT /note="Fumarate reductase subunit C"
FT /id="PRO_0000196526"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TRANSMEM 22..49
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TOPO_DOM 50..65
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TRANSMEM 66..90
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TOPO_DOM 91..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TRANSMEM 105..128
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10373108"
FT TOPO_DOM 129..131
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0000269|PubMed:15919996"
FT BINDING 29..30
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000269|PubMed:10373108,
FT ECO:0007744|PDB:1L0V"
FT BINDING 87
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0007744|PDB:1L0V"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 33..51
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 68..90
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1KF6"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1KF6"
FT HELIX 107..129
FT /evidence="ECO:0007829|PDB:1KF6"
SQ SEQUENCE 131 AA; 15015 MW; 26FDF83A2EF8EF43 CRC64;
MTTKRKPYVR PMTSTWWKKL PFYRFYMLRE GTAVPAVWFS IELIFGLFAL KNGPEAWAGF
VDFLQNPVIV IINLITLAAA LLHTKTWFEL APKAANIIVK DEKMGPEPII KSLWAVTVVA
TIVILFVALY W
