ID E7G575_9HELI Unreviewed; 255 AA.
AC E7G575;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Fumarate reductase cytochrome b subunit {ECO:0000256|PIRNR:PIRNR000177};
GN Name=fdrC {ECO:0000313|EMBL:EFX41440.1};
GN ORFNames=HSUHS5_1158 {ECO:0000313|EMBL:EFX41440.1};
OS Helicobacter suis HS5.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41440.1, ECO:0000313|Proteomes:UP000054093};
RN [1] {ECO:0000313|EMBL:EFX41440.1, ECO:0000313|Proteomes:UP000054093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS5 {ECO:0000313|EMBL:EFX41440.1,
RC ECO:0000313|Proteomes:UP000054093};
RX PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT "Genome sequence of Helicobacter suis supports its role in gastric
RT pathology.";
RL Vet. Res. 42:51-51(2011).
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:EFX41440.1}.
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DR EMBL; ADHO01000259; EFX41440.1; -; Genomic_DNA.
DR RefSeq; WP_006564837.1; NZ_ADHO01000259.1.
DR AlphaFoldDB; E7G575; -.
DR GeneID; 56929268; -.
DR Proteomes; UP000054093; 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 CDD; cd00581; QFR_TypeB_TM; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000054093};
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 28..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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:0000256|PIRSR:PIRSR000177-1"
FT BINDING 93
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 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:0000256|PIRSR:PIRSR000177-1"
FT BINDING 182
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 255 AA; 28768 MW; D7E5272A82901832 CRC64;
MQQEEIIEGY YGVSTERRKS GIYAKLDFLQ SATGLILALF MIAHMFLVSS ILISDKAMET
VTKFFEGSFL IKAGEPAIVS VVAAGVIVIL VAHAFLAMRK FPINYRQYQI FKTHKHLMAH
GDTSLWMVQA GTGFAMFFLA SIHLFVMLTQ PSSIGPHASS YRFVTQHFWL LYIFLLISVE
LHGSIGLYRL AIKWGWFKDL GIEQLRKIKW GMSVFFIVLG LLTYAAYIKK GIAGKEAGIT
TMQQAKQADE KLHKD
//
