ID B9D0E5_CAMRE Unreviewed; 237 AA.
AC B9D0E5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Fumarate reductase cytochrome b subunit {ECO:0000256|PIRNR:PIRNR000177};
GN ORFNames=CAMRE0001_1147 {ECO:0000313|EMBL:EEF14540.1};
OS Campylobacter rectus RM3267.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF14540.1, ECO:0000313|Proteomes:UP000003082};
RN [1] {ECO:0000313|EMBL:EEF14540.1, ECO:0000313|Proteomes:UP000003082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM3267 {ECO:0000313|EMBL:EEF14540.1,
RC ECO:0000313|Proteomes:UP000003082};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR000177}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR000177}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEF14540.1}.
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DR EMBL; ACFU01000006; EEF14540.1; -; Genomic_DNA.
DR RefSeq; WP_002944499.1; NZ_ACFU01000006.1.
DR AlphaFoldDB; B9D0E5; -.
DR STRING; 553218.CAMRE0001_1147; -.
DR eggNOG; ENOG5032QPG; Bacteria.
DR OrthoDB; 5345350at2; -.
DR Proteomes; UP000003082; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 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; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000177};
KW Electron transport {ECO:0000256|PIRNR:PIRNR000177};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000177};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000177};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000177};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000177};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR000177};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000177}.
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 42
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:0000256|PIRSR:PIRSR000177-1"
FT BINDING 91
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:0000256|PIRSR:PIRSR000177-1"
FT BINDING 141
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:0000256|PIRSR:PIRSR000177-1"
FT BINDING 177
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:0000256|PIRSR:PIRSR000177-1"
SQ SEQUENCE 237 AA; 26931 MW; 2ED196D4B37C8CDD CRC64;
MSGLIEGFLG RQADTKKSRT PAVWDRWQSI TGLILACFIL CHMVFTSTIL FGKGAFNAVV
GFAEAKFLFG EATWWITNAI AAVIFAIFIT HAFLAMRKFP ANYRQYIMFR GHKDRMKHLD
TTLWWFQFLT GFALFFAASA HLVDIIFGGH VTADKSIMAF HRLEIFYFAL LVFMVVHAGV
GMYRLYVKWV SIDGVNKEEM LAKRNKAKTI IFAVFGVLAI IALISDFVWI SYEVAGH
//
