BDBC_OCEIH
ID BDBC_OCEIH Reviewed; 145 AA.
AC Q8ERY3;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Probable disulfide formation protein {ECO:0000255|HAMAP-Rule:MF_00287};
DE AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00287};
DE AltName: Full=Thiol-disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00287};
GN Name=bdbC {ECO:0000255|HAMAP-Rule:MF_00287}; OrderedLocusNames=OB1163;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13119.1; -; Genomic_DNA.
DR RefSeq; WP_011065563.1; NC_004193.1.
DR AlphaFoldDB; Q8ERY3; -.
DR STRING; 221109.22776845; -.
DR EnsemblBacteria; BAC13119; BAC13119; BAC13119.
DR KEGG; oih:OB1163; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_128688_0_0_9; -.
DR OMA; WVNYFGF; -.
DR OrthoDB; 1859420at2; -.
DR PhylomeDB; Q8ERY3; -.
DR Proteomes; UP000000822; 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..145
FT /note="Probable disulfide formation protein"
FT /id="PRO_0000059385"
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 69..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 38..41
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 100..106
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ SEQUENCE 145 AA; 16264 MW; 6C3DDFA336A72A35 CRC64;
MKKLTKKAEN LLLLIWVQAF LALAGSLFYS EVMNYVPCEL CWYQRILMYP LVLIYGVAAI
KKDISFALPG LFMSGIGLLV STYHYLVQHV SIFQEVGGAC SGSVPCNVIY VNYFGFISIP
FMAGVAFLII FVLHLLILRE QGRKA
