ID A0A1G9ZQC8_9BACI Unreviewed; 204 AA.
AC A0A1G9ZQC8;
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 / fumarate reductase cytochrome b subunit {ECO:0000313|EMBL:SDN23297.1};
GN ORFNames=SAMN05216498_1796 {ECO:0000313|EMBL:SDN23297.1};
OS Tenuibacillus multivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tenuibacillus.
OX NCBI_TaxID=237069 {ECO:0000313|EMBL:SDN23297.1, ECO:0000313|Proteomes:UP000199334};
RN [1] {ECO:0000313|EMBL:SDN23297.1, ECO:0000313|Proteomes:UP000199334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3442 {ECO:0000313|EMBL:SDN23297.1,
RC ECO:0000313|Proteomes:UP000199334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNIG01000003; SDN23297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ZQC8; -.
DR STRING; 237069.SAMN05216498_1796; -.
DR OrthoDB; 9789209at2; -.
DR Proteomes; UP000199334; 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 Reference proteome {ECO:0000313|Proteomes:UP000199334};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 28
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 70
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 113
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 156
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 204 AA; 23468 MW; A5CA4B3524C3CBD4 CRC64;
MADNREFFYR RLHSLLGVIP IGLFLMQHLT VNFFSTYGPE AFNNAAGFME NLPLRLGLEI
FVIYLPLLFH AIYGVFIAFT AEPNTIRYGF FRNWMFLVQR ITGILTLIFI AWHVWETRLA
NAIYGTEINF DLMASILSDP IMFWFYIIGV VSAVFHFANG LWSFFVTWGL TISPKSQLVM
TYITIAIFAV FTYMGISSLI AFAS
//
