ID   DSBB2_PSEAE             Reviewed;         169 AA.
AC   P57701; Q9I5Z8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Disulfide bond formation protein B 2;
DE   AltName: Full=Disulfide oxidoreductase 2;
GN   Name=dsbB2; OrderedLocusNames=PA0538;
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 [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; AE004091; AAG03927.1; -; Genomic_DNA.
DR   PIR; E83578; E83578.
DR   RefSeq; NP_249229.1; NC_002516.2.
DR   RefSeq; WP_003113232.1; NZ_QZGE01000010.1.
DR   AlphaFoldDB; P57701; -.
DR   STRING; 287.DR97_3507; -.
DR   PaxDb; P57701; -.
DR   PRIDE; P57701; -.
DR   DNASU; 878500; -.
DR   EnsemblBacteria; AAG03927; AAG03927; PA0538.
DR   GeneID; 878500; -.
DR   KEGG; pae:PA0538; -.
DR   PATRIC; fig|208964.12.peg.570; -.
DR   PseudoCAP; PA0538; -.
DR   HOGENOM; CLU_098660_1_1_6; -.
DR   InParanoid; P57701; -.
DR   OMA; CGYDNPI; -.
DR   PhylomeDB; P57701; -.
DR   BioCyc; PAER208964:G1FZ6-544-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..169
FT                   /note="Disulfide bond formation protein B 2"
FT                   /id="PRO_0000059351"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..48
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..145
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..131
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   169 AA;  18132 MW;  C1088F7C362711F8 CRC64;
     MSALLKPLDN RLFWPAVAIG GLLILAFVLY LQHVRGFAPC SLCIFIRLDV LGLVLAGIVG
     SLAPRSRIAG GIAALGMLAA SLGGIYHAWS LVAEEKLAAQ GMGSCKMFMG FPEWIPLDTW
     LPQVFQPEGL CGEVVWTLLG QSMAVWSLAL FVFCLLVLAA KLAFGRRTA