DSBB_XANOM
ID DSBB_XANOM Reviewed; 172 AA.
AC Q2P728;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Disulfide bond formation protein B {ECO:0000255|HAMAP-Rule:MF_00286};
DE AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00286};
GN Name=dsbB {ECO:0000255|HAMAP-Rule:MF_00286}; OrderedLocusNames=XOO0894;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by oxidizing the DsbA protein. {ECO:0000255|HAMAP-
CC Rule:MF_00286}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00286}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00286}.
CC -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000255|HAMAP-
CC Rule:MF_00286}.
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DR EMBL; AP008229; BAE67649.1; -; Genomic_DNA.
DR RefSeq; WP_011407706.1; NC_007705.1.
DR AlphaFoldDB; Q2P728; -.
DR SMR; Q2P728; -.
DR KEGG; xom:XOO0894; -.
DR HOGENOM; CLU_098660_1_1_6; -.
DR OMA; GGALYMQ; -.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..172
FT /note="Disulfide bond formation protein B"
FT /id="PRO_0000298424"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 29..46
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 47..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 64..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 89..145
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 165..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT DISULFID 38..41
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT DISULFID 104..131
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ SEQUENCE 172 AA; 18886 MW; 959A2F581ADAB364 CRC64;
MNPFRWSFRA QFLLGFLACA GLLAYAIYVQ LHLGLEPCPL CIFQRIAFAA LAVFFLIGAL
HGPRAAGARK VYGVLSFIAA GVGMGIGARH VWVQIRPKDM MSSCGPPLSF LSETMGPFEV
FRTVLTGTGD CGNIDWRFLG LSMPMWSMVW FVGLALWALS AGFKARRSSL HH
