ID A0A099U0M1_9HELI Unreviewed; 278 AA.
AC A0A099U0M1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Fumarate reductase cytochrome b subunit {ECO:0000313|EMBL:STQ86066.1};
GN Name=frdC {ECO:0000313|EMBL:STQ86066.1};
GN ORFNames=LS73_002660 {ECO:0000313|EMBL:TLE01189.1}, NCTC12714_00857
GN {ECO:0000313|EMBL:STQ86066.1};
OS Helicobacter muridarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=216 {ECO:0000313|EMBL:STQ86066.1, ECO:0000313|Proteomes:UP000255139};
RN [1] {ECO:0000313|EMBL:TLE01189.1, ECO:0000313|Proteomes:UP000029922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:TLE01189.1,
RC ECO:0000313|Proteomes:UP000029922};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:STQ86066.1, ECO:0000313|Proteomes:UP000255139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ86066.1,
RC ECO:0000313|Proteomes:UP000255139};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UGJE01000002; STQ86066.1; -; Genomic_DNA.
DR EMBL; JRPD02000003; TLE01189.1; -; Genomic_DNA.
DR RefSeq; WP_034557785.1; NZ_UGJE01000002.1.
DR AlphaFoldDB; A0A099U0M1; -.
DR STRING; 216.LS73_04120; -.
DR OrthoDB; 5345350at2; -.
DR Proteomes; UP000029922; Unassembled WGS sequence.
DR Proteomes; UP000255139; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:InterPro.
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 Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000177-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000177-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000177-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255139};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..98
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 278 AA; 31821 MW; CBDA701EDE69C432 CRC64;
MQEDKIIEGY LGITPERKKS RMPARLDWWQ SATGLFLGLF MIAHMFFVSS ILISDEFMYT
ITKFFEGSIF IAAGEPKIVS GVAAFVFIVF VAHAFLAMRK FPINYRQFLA LKAHKHVMKH
SDTSLWFIQA ATGFVMFFLA SVHLYIMFAQ PDTIGPSGSS FRFFEQNFWL LYIVLLFAVE
LHGSIGLYRL CIKWGWLEGL GISGLRNAKW AMSAFFIILG LATFWAYFSK GMNQNFKDIN
DAKEYDHERF SKHAQSNLAN PDYMAKVAVS IAKENLSK
//
