ID A0A1H0QC99_9BACL Unreviewed; 212 AA.
AC A0A1H0QC99;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Succinate dehydrogenase subunit C {ECO:0000313|EMBL:SDP14992.1};
GN ORFNames=SAMN04487897_14021 {ECO:0000313|EMBL:SDP14992.1};
OS Paenibacillus sp. yr247.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDP14992.1, ECO:0000313|Proteomes:UP000198936};
RN [1] {ECO:0000313|EMBL:SDP14992.1, ECO:0000313|Proteomes:UP000198936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR247 {ECO:0000313|EMBL:SDP14992.1,
RC ECO:0000313|Proteomes:UP000198936};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNIF01000040; SDP14992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0QC99; -.
DR STRING; 1761880.SAMN04487897_14021; -.
DR OrthoDB; 9789209at2; -.
DR Proteomes; UP000198936; 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:UP000198936};
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..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..204
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 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 158
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 212 AA; 24296 MW; 60DA53B8669D8FE9 CRC64;
MKGNSYYWRK LHSLLGVIPL GGFILVHVSI NFQAFERGPE GFTNYVHFIN SLPLKPLLEI
FGIYLPILFH GIYGLYMAYQ SNLNSGQYTY GRNWAFTLQR ITGVLTFIFV FWHFFNTRLQ
VYLGSITHEE LGSTMHQIAM NPVLFIIYVI GVLSAVFHFS NGLWAFLISW GITISPRSQK
ISSYICMGVF VLISLLFFLS LVAFTGDNSK YE
//
