ID   BDBB_BPSPB              Reviewed;         148 AA.
AC   P68572; O31985; O64037;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   29-SEP-2021, entry version 67.
DE   RecName: Full=Disulfide bond formation protein B;
DE   AltName: Full=Thiol-disulfide oxidoreductase B;
DE            Short=Disulfide oxidoreductase B;
GN   Name=bdbB; OrderedLocusNames=SPBc2p024;
OS   Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Spbetavirus.
OX   NCBI_TaxID=66797;
OH   NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10376821; DOI=10.1099/13500872-145-5-1055;
RA   Lazarevic V., Duesterhoeft A., Soldo B., Hilbert H., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the Bacillus subtilis temperate bacteriophage
RT   SPbetac2.";
RL   Microbiology 145:1055-1067(1999).
CC   -!- FUNCTION: Important but not absolutely essential for the production of
CC       the lantibiotic sublancin 168, it may also be required for the
CC       stability of other secreted proteins. Not required for competence for
CC       DNA uptake (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily. {ECO:0000305}.
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DR   EMBL; AF020713; AAC12996.1; -; Genomic_DNA.
DR   PIR; T12787; T12787.
DR   RefSeq; NP_046575.1; NC_001884.1.
DR   GeneID; 1261374; -.
DR   KEGG; vg:1261374; -.
DR   Proteomes; UP000009091; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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   Chaperone; Disulfide bond; Electron transport; Host membrane; Membrane;
KW   Oxidoreductase; Redox-active center; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..148
FT                   /note="Disulfide bond formation protein B"
FT                   /id="PRO_0000059378"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..39
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..102
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  17139 MW;  25676A3B9C9AF6DC CRC64;
     MNTRYVKSFF LLLFFLSFFG TMASLFYSEI MHFKPCVLCW YQRIFLYPIP IILLIGLLKK
     DLNSIFYVVF LSSIGLIIAF YHYIIQLTQS KSVVCEIGTN SCAKIEVEYL GFITLPLMSS
     VCFALIFGIG LKLIIKSKKL KQNQHVYN