DSBB1_PSEAE
ID DSBB1_PSEAE Reviewed; 163 AA.
AC P21482; Q9HTT9;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Disulfide bond formation protein B 1;
DE AltName: Full=Disulfide oxidoreductase 1;
GN Name=dsbB1; OrderedLocusNames=PA5256;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2514124; DOI=10.1016/0378-1119(89)90136-4;
RA Kato J., Chu L., Kitano K., Devault J.D., Kimbara K., Chakrabarty A.M.,
RA Misra T.K.;
RT "Nucleotide sequence of a regulatory region controlling alginate synthesis
RT in Pseudomonas aeruginosa: characterization of the algR2 gene.";
RL Gene 84:31-38(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by oxidizing the DsbA protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000305}.
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DR EMBL; M30145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE004091; AAG08641.1; -; Genomic_DNA.
DR PIR; F82988; F82988.
DR PIR; JQ0144; JQ0144.
DR RefSeq; NP_253943.1; NC_002516.2.
DR RefSeq; WP_003099230.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; P21482; -.
DR SMR; P21482; -.
DR STRING; 287.DR97_2627; -.
DR PaxDb; P21482; -.
DR DNASU; 879720; -.
DR EnsemblBacteria; AAG08641; AAG08641; PA5256.
DR GeneID; 879720; -.
DR KEGG; pae:PA5256; -.
DR PATRIC; fig|208964.12.peg.5509; -.
DR PseudoCAP; PA5256; -.
DR HOGENOM; CLU_098660_1_1_6; -.
DR InParanoid; P21482; -.
DR OMA; GGALYMQ; -.
DR PhylomeDB; P21482; -.
DR BioCyc; PAER208964:G1FZ6-5377-MON; -.
DR Proteomes; UP000002438; 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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IMP:PseudoCAP.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00286; DsbB; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR022920; Disulphide_bond_form_DsbB.
DR InterPro; IPR023380; DsbB-like_sf.
DR Pfam; PF02600; DsbB; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW Electron transport; Membrane; Oxidoreductase; Redox-active center;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..163
FT /note="Disulfide bond formation protein B 1"
FT /id="PRO_0000059350"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..44
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..142
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 36..39
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 101..128
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 163
FT /note="A -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 17764 MW; B77C7F7A5F04025E CRC64;
MPLASPRQLF LLAFLACVAI MGGALYLEHV VGLEACPLCV VQRIFFILIG LTCLAGAIQG
PGLRGRRIYS VLVFLLALGG GATAARQVWL QTVPLDQLPA CLPSLDYMMQ ALPFQEVIRL
VLHGTADCAQ VSWTLFTLSI PEWSLLAFVA YLGFSIVQFL RRA
