ID   DSBB_BURCE     STANDARD;      PRT;   170 AA.
AC   P94287;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Disulfide bond formation protein B (Disulfide oxidoreductase).
GN   Name=dsbB;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KF1;
RX   MEDLINE=97047727; PubMed=8926116;
RA   Abe M., Nakazawa T.;
RT   "The dsbB gene product is required for protease production by
RT   Burkholderia cepacia.";
RL   Infect. Immun. 64:4378-4380(1996).
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by oxidizing the dsbA protein (By
CC       similarity). Required for the production of extracellular
CC       protease.
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein. Inner membrane
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the dsbB family.
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CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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DR   EMBL; D83234; BAA11858.1; -.
DR   HAMAP; MF_00286; -; 1.
DR   InterPro; IPR003752; DsbB.
DR   Pfam; PF02600; DsbB; 1.
KW   Chaperone; Electron transport; Inner membrane; Oxidoreductase;
KW   Redox-active center; Transmembrane; Transport.
FT   DOMAIN        1     14       Cytoplasmic (Potential).
FT   TRANSMEM     15     31       Potential.
FT   DOMAIN       32     49       Periplasmic (Potential).
FT   TRANSMEM     50     64       Potential.
FT   DOMAIN       65     71       Cytoplasmic (Potential).
FT   TRANSMEM     72     89       Potential.
FT   DOMAIN       90    144       Periplasmic (Potential).
FT   TRANSMEM    145    163       Potential.
FT   DOMAIN      164    170       Cytoplasmic (Potential).
FT   DISULFID     41     44       Redox-active (By similarity).
FT   DISULFID    102    130       Redox-active (By similarity).
SQ   SEQUENCE   170 AA;  18765 MW;  BCC1918444BDFC6B CRC64;
     MNDYTLALRR ERRLLMLLGW VCIALLAGAL YLQYVKNEDP CPLCIIQRYF FCAIGIFAFV
     AAGIRNWRGV WVLELLIAIA AAGGVGTAAR HLSIQMNPGF SCGFDTLQPI VDSLPPAQWF
     PGMFKVAGLC ETVYPPIFGI LLPGWALIGF AVILVAVVAS LWRHRRKLAS
//