FRDC_HELPY
ID FRDC_HELPY Reviewed; 255 AA.
AC O06912;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Fumarate reductase cytochrome b subunit;
DE AltName: Full=Quinol-fumarate reductase cytochrome b subunit {ECO:0000305};
DE Short=QFR cytochrome b subunit {ECO:0000305};
GN Name=frdC; OrderedLocusNames=HP_0193;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX PubMed=9434188; DOI=10.1016/s0378-1119(97)00550-7;
RA Ge Z., Jiang Q., Kalisiak M.S., Taylor D.E.;
RT "Cloning and functional characterization of Helicobacter pylori fumarate
RT reductase operon comprising three structural genes coding for subunits C, A
RT and B.";
RL Gene 204:227-234(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: The fumarate reductase enzyme complex is required for
CC fumarate respiration. This subunit anchors the complex in the membrane
CC and binds a diheme cytochrome b. {ECO:0000250|UniProtKB:P17413}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P17413};
CC Note=Binds 2 heme b molecules per subunit, called the proximal (bP) and
CC distal (bD) hemes. {ECO:0000250|UniProtKB:P17413};
CC -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC flavoprotein (frdA), an iron-sulfur protein (frdB), and diheme
CC cytochrome b (frdC). {ECO:0000250|UniProtKB:P17413}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P17413}.
CC -!- SIMILARITY: Belongs to the diheme cytochrome b FrdC family.
CC {ECO:0000305}.
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DR EMBL; U78101; AAC46063.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07260.1; -; Genomic_DNA.
DR PIR; A64544; A64544.
DR RefSeq; NP_206992.1; NC_000915.1.
DR RefSeq; WP_001183634.1; NC_018939.1.
DR AlphaFoldDB; O06912; -.
DR SMR; O06912; -.
DR STRING; 85962.C694_00960; -.
DR PaxDb; O06912; -.
DR EnsemblBacteria; AAD07260; AAD07260; HP_0193.
DR KEGG; hpy:HP_0193; -.
DR PATRIC; fig|85962.47.peg.208; -.
DR eggNOG; ENOG5031HUY; Bacteria.
DR OMA; LLAHLHF; -.
DR PhylomeDB; O06912; -.
DR BioCyc; MetaCyc:HP0193-MON; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00581; QFR_TypeB_TM; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR004224; Fum_red_B_TM.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000177; Fumar_rd_cyt_b; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..255
FT /note="Fumarate reductase cytochrome b subunit"
FT /id="PRO_0000158683"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bP"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT BINDING 143
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT BINDING 182
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bP"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT CONFLICT 86
FT /note="I -> V (in Ref. 1; AAC46063)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="L -> V (in Ref. 1; AAC46063)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="V -> A (in Ref. 1; AAC46063)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="E -> D (in Ref. 1; AAC46063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28886 MW; E74716D64957AD50 CRC64;
MQQEEIIEGY YGASKGLKKS GIYAKLDFLQ SATGLILALF MIAHMFLVSS ILISDEAMYK
VAKFFEGSLF LKAGEPAIVS VVAAGIILIL VAHAFLALRK FPINYRQYKV FKTHKHLMKH
GDTSLWFIQA LTGFAMFFLA SIHLFVMLTE PESIGPHGSS YRFVTQNFWL LYIFLLFAVE
LHGSIGLYRL AIKWGWFKNV SIQGLRKVKW AMSVFFIVLG LCTYGAYIKK GLENKENGIK
TMQEAIEADG KFHKE
