DSBB_ECOLI
ID DSBB_ECOLI Reviewed; 176 AA.
AC P0A6M2; P30018; Q47408;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Disulfide bond formation protein B;
DE AltName: Full=Disulfide oxidoreductase;
GN Name=dsbB; Synonyms=roxB, ycgA; OrderedLocusNames=b1185, JW5182;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8430071; DOI=10.1073/pnas.90.3.1038;
RA Bardwell J.C.A., Lee J.-O., Jander G., Martin N., Belin D., Beckwith J.;
RT "A pathway for disulfide bond formation in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1038-1042(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7688471; DOI=10.1073/pnas.90.15.7084;
RA Missiakas D., Georgopoulos C., Raina S.;
RT "Identification and characterization of the Escherichia coli gene dsbB,
RT whose product is involved in the formation of disulfide bonds in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7084-7088(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
RC STRAIN=K12;
RX PubMed=1317851; DOI=10.1016/s0021-9258(19)49875-x;
RA Pinner E., Padan E., Schuldiner S.;
RT "Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+
RT antiporter in Escherichia coli.";
RL J. Biol. Chem. 267:11064-11068(1992).
RN [7]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYSTEINE RESIDUES.
RX PubMed=7957076; DOI=10.1002/j.1460-2075.1994.tb06841.x;
RA Jander G., Martin N.L., Beckwith J.;
RT "Two cysteines in each periplasmic domain of the membrane protein DsbB are
RT required for its function in protein disulfide bond formation.";
RL EMBO J. 13:5121-5127(1994).
RN [8]
RP REDOX-ACTIVE SITES, AND DISULFIDE BONDS.
RX PubMed=10064586; DOI=10.1093/emboj/18.5.1192;
RA Kobayashi T., Ito K.;
RT "Respiratory chain strongly oxidizes the CXXC motif of DsbB in the
RT Escherichia coli disulfide bond formation pathway.";
RL EMBO J. 18:1192-1198(1999).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP FUNCTION IN PHOP/PHOQ REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22267510; DOI=10.1128/jb.06055-11;
RA Lippa A.M., Goulian M.;
RT "Perturbation of the oxidizing environment of the periplasm stimulates the
RT PhoQ/PhoP system in Escherichia coli.";
RL J. Bacteriol. 194:1457-1463(2012).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein.
CC PhoP-regulated transcription is redox-sensitive, being activated when
CC the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment
CC with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this
CC pathway. {ECO:0000269|PubMed:22267510, ECO:0000269|PubMed:7688471,
CC ECO:0000269|PubMed:8430071}.
CC -!- INTERACTION:
CC P0A6M2; P0AEG4: dsbA; NbExp=5; IntAct=EBI-1170740, EBI-549711;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7957076,
CC ECO:0000269|PubMed:8430071}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7957076, ECO:0000269|PubMed:8430071}.
CC -!- DISRUPTION PHENOTYPE: Induction of the PhoP/PhoQ two-component
CC regulatory system. {ECO:0000269|PubMed:22267510}.
CC -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23711.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA24220.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L03721; AAA23711.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74269.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36032.2; -; Genomic_DNA.
DR EMBL; M83655; AAA24220.1; ALT_FRAME; Genomic_DNA.
DR PIR; F64864; F64864.
DR RefSeq; NP_415703.3; NC_000913.3.
DR RefSeq; WP_000943459.1; NZ_SSZK01000010.1.
DR PDB; 2HI7; X-ray; 3.70 A; B=1-176.
DR PDB; 2K73; NMR; -; A=1-176.
DR PDB; 2K74; NMR; -; A=1-176.
DR PDB; 2LEG; NMR; -; B=1-176.
DR PDB; 2LTQ; NMR; -; A/D=1-176.
DR PDB; 2ZUP; X-ray; 3.70 A; B=1-176.
DR PDB; 2ZUQ; X-ray; 3.30 A; A/D=1-176.
DR PDB; 3E9J; X-ray; 3.70 A; C/F=1-176.
DR PDB; 6WVF; X-ray; 2.90 A; A=7-167.
DR PDBsum; 2HI7; -.
DR PDBsum; 2K73; -.
DR PDBsum; 2K74; -.
DR PDBsum; 2LEG; -.
DR PDBsum; 2LTQ; -.
DR PDBsum; 2ZUP; -.
DR PDBsum; 2ZUQ; -.
DR PDBsum; 3E9J; -.
DR PDBsum; 6WVF; -.
DR AlphaFoldDB; P0A6M2; -.
DR BMRB; P0A6M2; -.
DR SMR; P0A6M2; -.
DR BioGRID; 4261815; 428.
DR IntAct; P0A6M2; 1.
DR MINT; P0A6M2; -.
DR STRING; 511145.b1185; -.
DR BindingDB; P0A6M2; -.
DR DrugBank; DB08689; Ubiquinone Q1.
DR DrugBank; DB08690; Ubiquinone Q2.
DR TCDB; 5.A.2.1.1; the disulfide bond oxidoreductase b (dsbb) family.
DR jPOST; P0A6M2; -.
DR PaxDb; P0A6M2; -.
DR PRIDE; P0A6M2; -.
DR ABCD; P0A6M2; 1 sequenced antibody.
DR EnsemblBacteria; AAC74269; AAC74269; b1185.
DR EnsemblBacteria; BAA36032; BAA36032; BAA36032.
DR GeneID; 66674995; -.
DR GeneID; 946344; -.
DR KEGG; ecj:JW5182; -.
DR KEGG; eco:b1185; -.
DR PATRIC; fig|1411691.4.peg.1102; -.
DR EchoBASE; EB1366; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_098660_2_0_6; -.
DR InParanoid; P0A6M2; -.
DR OMA; GGALYMQ; -.
DR PhylomeDB; P0A6M2; -.
DR BioCyc; EcoCyc:DSBBPROT-MON; -.
DR BioCyc; MetaCyc:DSBBPROT-MON; -.
DR BRENDA; 1.8.5.9; 2026.
DR EvolutionaryTrace; P0A6M2; -.
DR PRO; PR:P0A6M2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IDA:EcoCyc.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IMP:EcoCyc.
DR GO; GO:0048039; F:ubiquinone binding; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone;
KW Disulfide bond; Electron transport; Membrane; Oxidoreductase;
KW Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..176
FT /note="Disulfide bond formation protein B"
FT /id="PRO_0000059342"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..31
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 32..49
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..65
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 66..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 90..144
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..163
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 164..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DISULFID 41..44
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:10064586"
FT DISULFID 104..130
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:10064586"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:2K73"
FT HELIX 13..34
FT /evidence="ECO:0007829|PDB:6WVF"
FT HELIX 42..63
FT /evidence="ECO:0007829|PDB:6WVF"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2LEG"
FT HELIX 70..96
FT /evidence="ECO:0007829|PDB:6WVF"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6WVF"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6WVF"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6WVF"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6WVF"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2LTQ"
FT HELIX 142..167
FT /evidence="ECO:0007829|PDB:6WVF"
SQ SEQUENCE 176 AA; 20142 MW; 9CBD673D51E9F09B CRC64;
MLRFLNQCSQ GRGAWLLMAF TALALELTAL WFQHVMLLKP CVLCIYERCA LFGVLGAALI
GAIAPKTPLR YVAMVIWLYS AFRGVQLTYE HTMLQLYPSP FATCDFMVRF PEWLPLDKWV
PQVFVASGDC AERQWDFLGL EMPQWLLGIF IAYLIVAVLV VISQPFKAKK RDLFGR
