ID A0A1I4MW16_9BACI Unreviewed; 202 AA.
AC A0A1I4MW16;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Succinate dehydrogenase subunit C {ECO:0000313|EMBL:SFM07180.1};
GN ORFNames=SAMN04487943_107118 {ECO:0000313|EMBL:SFM07180.1};
OS Gracilibacillus orientalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=334253 {ECO:0000313|EMBL:SFM07180.1, ECO:0000313|Proteomes:UP000198565};
RN [1] {ECO:0000313|EMBL:SFM07180.1, ECO:0000313|Proteomes:UP000198565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.4250 {ECO:0000313|EMBL:SFM07180.1,
RC ECO:0000313|Proteomes:UP000198565};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOTR01000007; SFM07180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4MW16; -.
DR STRING; 334253.SAMN04487943_107118; -.
DR OrthoDB; 9789209at2; -.
DR Proteomes; UP000198565; 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 CDD; cd03497; SQR_TypeB_1_TM; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR011138; Cytochrome_b-558.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR016002; Succ_DH_cyt_b558_Firmicute.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR NCBIfam; TIGR02046; sdhC_b558_fam; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000170; Succ_dh_cyt_b558; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000170-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000170-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000170-1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 27
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
FT BINDING 112
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000170-1"
SQ SEQUENCE 202 AA; 23524 MW; 6027BE9B61B4F580 CRC64;
MENREFFYRR LHSLLGVVPI GIFLIQHLVV NHFAVYGPES FNRAAQFMHD LPFRLMLEIL
IIFLPIIFHA VLGVYIVFVA KNNVSRYGFF RNWLFYLQRI TGIITLVFIV WHVWETRVQI
GMGTEELNYG LMENILANPV MFWFYVIGVV STTFHFANGL WSFLVSWGVT VTPRSQKIAT
YATLLVFLAV TYIGIRALFA FV
//
