DSBD_ECOLI
ID DSBD_ECOLI Reviewed; 565 AA.
AC P36655; P76796; Q2M6G8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Thiol:disulfide interchange protein DsbD;
DE EC=1.8.1.8;
DE AltName: Full=C-type cytochrome biogenesis protein CycZ;
DE AltName: Full=Inner membrane copper tolerance protein;
DE AltName: Full=Protein-disulfide reductase;
DE Short=Disulfide reductase;
DE Flags: Precursor;
GN Name=dsbD; Synonyms=cutA2, cycZ, dipZ; OrderedLocusNames=b4136, JW5734;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=7628442; DOI=10.1002/j.1460-2075.1995.tb07347.x;
RA Missiakas D., Schwager F., Raina S.;
RT "Identification and characterization of a new disulfide isomerase-like
RT protein (DsbD) in Escherichia coli.";
RL EMBO J. 14:3415-3424(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7623666; DOI=10.1111/j.1365-2958.1995.tb02286.x;
RA Fong S.-T., Camakaris J., Lee B.T.O.;
RT "Molecular genetics of a chromosomal locus involved in copper tolerance in
RT Escherichia coli K-12.";
RL Mol. Microbiol. 15:1127-1137(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7623667; DOI=10.1111/j.1365-2958.1995.tb02287.x;
RA Crooke H.R., Cole J.A.;
RT "The biogenesis of c-type cytochromes in Escherichia coli requires a
RT membrane-bound protein, DipZ, with a protein disulphide isomerase-like
RT domain.";
RL Mol. Microbiol. 15:1139-1150(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 2-8 (PRECURSOR PROTEIN), PROTEIN SEQUENCE OF 20-34,
RP TOPOLOGY, AND MUTAGENESIS OF CYS-122; CYS-128; CYS-182; CYS-301; CYS-304;
RP CYS-480 AND CYS-483.
RX PubMed=10760137; DOI=10.1046/j.1365-2958.2000.01796.x;
RA Gordon E.H.J., Page M.D., Willis A.C., Ferguson S.J.;
RT "Escherichia coli DipZ: anatomy of a transmembrane protein disulphide
RT reductase in which three pairs of cysteine residues, one in each of three
RT domains, contribute differentially to function.";
RL Mol. Microbiol. 35:1360-1374(2000).
RN [8]
RP PROTEIN SEQUENCE OF 20-27, TOPOLOGY, AND MUTAGENESIS OF CYS-122; CYS-128;
RP CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483.
RC STRAIN=BL21-DE3;
RX PubMed=10712691; DOI=10.1046/j.1365-2958.2000.01778.x;
RA Chung J., Chen T., Missiakas D.;
RT "Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane
RT protein involved in thiol-disulphide exchange and protein folding in the
RT bacterial periplasm.";
RL Mol. Microbiol. 35:1099-1109(2000).
RN [9]
RP PROTEIN SEQUENCE OF 78-82.
RA Missiakas D., Hughes G.J., Frutiger S., Paquet N., Raina S.;
RL Submitted (MAY-1995) to UniProtKB.
RN [10]
RP CHARACTERIZATION.
RX PubMed=7957865; DOI=10.1016/0014-5793(94)01053-6;
RA Sambongi Y., Ferguson S.J.;
RT "Specific thiol compounds complement deficiency in c-type cytochrome
RT biogenesis in Escherichia coli carrying a mutation in a membrane-bound
RT disulphide isomerase-like protein.";
RL FEBS Lett. 353:235-238(1994).
RN [11]
RP TOPOLOGY, AND MUTAGENESIS OF CYS-13; CYS-122; CYS-128; CYS-182; CYS-301;
RP CYS-304; CYS-480 AND CYS-483.
RC STRAIN=DHB4, and RI242;
RX PubMed=10545108; DOI=10.1093/emboj/18.21.5963;
RA Stewart E.J., Katzen F., Beckwith J.;
RT "Six conserved cysteines of the membrane protein DsbD are required for the
RT transfer of electrons from the cytoplasm to the periplasm of Escherichia
RT coli.";
RL EMBO J. 18:5963-5971(1999).
RN [12]
RP CHARACTERIZATION.
RX PubMed=11114333; DOI=10.1016/s0092-8674(00)00180-x;
RA Katzen F., Beckwith J.;
RT "Transmembrane electron transfer by the membrane protein DsbD occurs via a
RT disulfide bond cascade.";
RL Cell 103:769-779(2000).
RN [13]
RP CHARACTERIZATION.
RC STRAIN=K38;
RX PubMed=11085993; DOI=10.1074/jbc.m009500200;
RA Krupp R., Chan C., Missiakas D.;
RT "DsbD-catalyzed transport of electrons across the membrane of Escherichia
RT coli.";
RL J. Biol. Chem. 276:3696-3701(2001).
RN [14]
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).
CC -!- FUNCTION: Required to facilitate the formation of correct disulfide
CC bonds in some periplasmic proteins and for the assembly of the
CC periplasmic c-type cytochromes. Acts by transferring electrons from
CC cytoplasmic thioredoxin to the periplasm, thereby maintaining the
CC active site of DsbC, DsbE and DsbG in a reduced state. This transfer
CC involves a cascade of disulfide bond formation and reduction steps.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC -!- INTERACTION:
CC P36655; P0AA86: dsbE; NbExp=4; IntAct=EBI-9014057, EBI-9014059;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: The consequences of replacement of the cysteines with
CC alanines were found to depend on the conditions tested and on the
CC reporter system used for the analysis, and then differ depending on the
CC references.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA54781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA85375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z36905; CAA85375.1; ALT_INIT; Genomic_DNA.
DR EMBL; X77707; CAA54781.1; ALT_INIT; Genomic_DNA.
DR EMBL; U14003; AAA97035.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77096.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78138.1; -; Genomic_DNA.
DR PIR; S56364; S56364.
DR RefSeq; NP_418559.1; NC_000913.3.
DR RefSeq; WP_000068922.1; NZ_SSZK01000018.1.
DR PDB; 1JPE; X-ray; 1.90 A; A=20-151.
DR PDB; 1JZD; X-ray; 2.30 A; C=20-151.
DR PDB; 1L6P; X-ray; 1.65 A; A=20-144.
DR PDB; 1VRS; X-ray; 2.85 A; A/B/C=20-162, D/E/F=438-565.
DR PDB; 1Z5Y; X-ray; 1.94 A; D=20-162.
DR PDB; 2FWE; X-ray; 1.65 A; A=438-565.
DR PDB; 2FWF; X-ray; 1.30 A; A=438-565.
DR PDB; 2FWG; X-ray; 1.10 A; A=438-565.
DR PDB; 2FWH; X-ray; 0.99 A; A=438-565.
DR PDB; 3PFU; X-ray; 1.80 A; A=21-151.
DR PDB; 4IP1; X-ray; 2.47 A; A=444-565.
DR PDB; 4IP6; X-ray; 2.23 A; A=444-565.
DR PDB; 5NHI; X-ray; 2.60 A; A/B=21-151.
DR PDBsum; 1JPE; -.
DR PDBsum; 1JZD; -.
DR PDBsum; 1L6P; -.
DR PDBsum; 1VRS; -.
DR PDBsum; 1Z5Y; -.
DR PDBsum; 2FWE; -.
DR PDBsum; 2FWF; -.
DR PDBsum; 2FWG; -.
DR PDBsum; 2FWH; -.
DR PDBsum; 3PFU; -.
DR PDBsum; 4IP1; -.
DR PDBsum; 4IP6; -.
DR PDBsum; 5NHI; -.
DR AlphaFoldDB; P36655; -.
DR BMRB; P36655; -.
DR SMR; P36655; -.
DR BioGRID; 4262691; 1010.
DR DIP; DIP-9476N; -.
DR IntAct; P36655; 1.
DR STRING; 511145.b4136; -.
DR TCDB; 5.A.1.1.1; the disulfide bond oxidoreductase d (dsbd) family.
DR PaxDb; P36655; -.
DR PRIDE; P36655; -.
DR EnsemblBacteria; AAC77096; AAC77096; b4136.
DR EnsemblBacteria; BAE78138; BAE78138; BAE78138.
DR GeneID; 948649; -.
DR KEGG; ecj:JW5734; -.
DR KEGG; eco:b4136; -.
DR PATRIC; fig|511145.12.peg.4267; -.
DR EchoBASE; EB2095; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_0_6; -.
DR InParanoid; P36655; -.
DR OMA; YRHRFQF; -.
DR PhylomeDB; P36655; -.
DR BioCyc; EcoCyc:DSBD-MON; -.
DR BioCyc; MetaCyc:DSBD-MON; -.
DR BRENDA; 1.8.4.16; 2026.
DR EvolutionaryTrace; P36655; -.
DR PRO; PR:P36655; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:EcoCyc.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0046688; P:response to copper ion; IMP:EcoCyc.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 2.60.40.1250; -; 1.
DR HAMAP; MF_00399; DbsD; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR022910; Thiol_diS_interchange_DbsD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
DR Pfam; PF11412; DsbC; 1.
DR Pfam; PF02683; DsbD; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF74863; SSF74863; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cytochrome c-type biogenesis; Direct protein sequencing; Disulfide bond;
KW Electron transport; Membrane; NAD; Oxidoreductase; Redox-active center;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10712691,
FT ECO:0000269|PubMed:10760137"
FT CHAIN 20..565
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007373"
FT TOPO_DOM 20..162
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..242
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..322
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..383
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..565
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 434..565
FT /note="Thioredoxin"
FT DISULFID 122..128
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT DISULFID 182..304
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT DISULFID 480..483
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT MUTAGEN 13
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:10545108"
FT MUTAGEN 122
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT MUTAGEN 128
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT MUTAGEN 182
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT MUTAGEN 301
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT MUTAGEN 304
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT MUTAGEN 480
FT /note="C->A: Loss of activity; when associated with A-483."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT MUTAGEN 483
FT /note="C->A: Loss of activity; when associated with A-480."
FT /evidence="ECO:0000269|PubMed:10545108,
FT ECO:0000269|PubMed:10712691, ECO:0000269|PubMed:10760137"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1L6P"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1L6P"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1L6P"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 98..119
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1L6P"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1L6P"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1L6P"
FT HELIX 456..466
FT /evidence="ECO:0007829|PDB:2FWH"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:2FWH"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:2FWH"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:2FWH"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:2FWH"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:2FWH"
FT STRAND 503..509
FT /evidence="ECO:0007829|PDB:2FWH"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:2FWH"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:2FWH"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:2FWH"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:1VRS"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:2FWH"
SQ SEQUENCE 565 AA; 61795 MW; 41EFAA1C9EAC6C5F CRC64;
MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPADQAFAFD FQQNQHDLNL TWQIKDGYYL
YRKQIRITPE HAKIADVQLP QGVWHEDEFY GKSEIYRDRL TLPVTINQAS AGATLTVTYQ
GCADAGFCYP PETKTVPLSE VVANNAAPQP VSVPQQEQPT AQLPFSALWA LLIGIGIAFT
PCVLPMYPLI SGIVLGGKQR LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ
HPYVLIGLAI VFTLLAMSMF GLFTLQLPSS LQTRLTLMSN RQQGGSPGGV FVMGAIAGLI
CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL LPKSGPWMEQ
VKTAFGFVIL ALPVFLLERV IGDVWGLRLW SALGVAFFGW AFITSLQAKR GWMRIVQIIL
LAAALVSVRP LQDWAFGATH TAQTQTHLNF TQIKTVDELN QALVEAKGKP VMLDLYADWC
VACKEFEKYT FSDPQVQKAL ADTVLLQANV TANDAQDVAL LKHLNVLGLP TILFFDGQGQ
EHPQARVTGF MDAETFSAHL RDRQP
