BDBC_ALKHC
ID BDBC_ALKHC Reviewed; 137 AA.
AC Q9KBI6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Probable disulfide formation protein C {ECO:0000255|HAMAP-Rule:MF_00287};
DE AltName: Full=Disulfide oxidoreductase C {ECO:0000255|HAMAP-Rule:MF_00287};
DE AltName: Full=Thiol-disulfide oxidoreductase C {ECO:0000255|HAMAP-Rule:MF_00287};
GN Name=bdbC {ECO:0000255|HAMAP-Rule:MF_00287}; OrderedLocusNames=BH1941;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00287}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00287};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00287}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00287}.
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DR EMBL; BA000004; BAB05660.1; -; Genomic_DNA.
DR PIR; E83892; E83892.
DR RefSeq; WP_010898100.1; NC_002570.2.
DR AlphaFoldDB; Q9KBI6; -.
DR STRING; 272558.10174559; -.
DR EnsemblBacteria; BAB05660; BAB05660; BAB05660.
DR KEGG; bha:BH1941; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_128688_0_0_9; -.
DR OMA; INWFGFI; -.
DR OrthoDB; 1859420at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00287; BdbC; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR012187; Disulphide_bond_form_BdbC.
DR InterPro; IPR023380; DsbB-like_sf.
DR PANTHER; PTHR43469; PTHR43469; 1.
DR Pfam; PF02600; DsbB; 1.
DR PIRSF; PIRSF036659; BdbC; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chaperone; Disulfide bond; Electron transport; Membrane;
KW Oxidoreductase; Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..137
FT /note="Probable disulfide formation protein C"
FT /id="PRO_0000059375"
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 35..38
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 97..102
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ SEQUENCE 137 AA; 15870 MW; 61B4F4C869BEEEA7 CRC64;
MSKKVENLML GSWLTALTAM LGSLYFSEIR MYEPCTLCWY QRIIMYPLVL ILFIGYLKRD
VNVALYSLWF SLIGMFTSLY HYSIQKLPFL TDAAPACGRV PCTGQYINWF GFVTIPFLAF
TAFVIIFICS LLIIREK
