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Thiol:disulfide interchange protein DsbD (EC 1.8.1.8) (C-type cytochrome biogenesis protein CycZ) (Inner membrane copper tolerance protein) (Protein-disulfide reductase) (Disulfide reductase)

 DSBD_ECOLI              Reviewed;         565 AA.
P36655; P76796; Q2M6G8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 4.
10-OCT-2018, entry version 181.
RecName: Full=Thiol:disulfide interchange protein DsbD;
EC=1.8.1.8;
AltName: Full=C-type cytochrome biogenesis protein CycZ;
AltName: Full=Inner membrane copper tolerance protein;
AltName: Full=Protein-disulfide reductase;
Short=Disulfide reductase;
Flags: Precursor;
Name=dsbD; Synonyms=cutA2, cycZ, dipZ;
OrderedLocusNames=b4136, JW5734;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
PubMed=7628442;
Missiakas D., Schwager F., Raina S.;
"Identification and characterization of a new disulfide isomerase-like
protein (DsbD) in Escherichia coli.";
EMBO J. 14:3415-3424(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7623666; DOI=10.1111/j.1365-2958.1995.tb02286.x;
Fong S.-T., Camakaris J., Lee B.T.O.;
"Molecular genetics of a chromosomal locus involved in copper
tolerance in Escherichia coli K-12.";
Mol. Microbiol. 15:1127-1137(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=7623667; DOI=10.1111/j.1365-2958.1995.tb02287.x;
Crooke H.R., Cole J.A.;
"The biogenesis of c-type cytochromes in Escherichia coli requires a
membrane-bound protein, DipZ, with a protein disulphide isomerase-like
domain.";
Mol. Microbiol. 15:1139-1150(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
PROTEIN SEQUENCE OF 2-8 (PRECURSOR PROTEIN), PROTEIN SEQUENCE OF
20-34, TOPOLOGY, AND MUTAGENESIS OF CYS-122; CYS-128; CYS-182;
CYS-301; CYS-304; CYS-480 AND CYS-483.
PubMed=10760137; DOI=10.1046/j.1365-2958.2000.01796.x;
Gordon E.H.J., Page M.D., Willis A.C., Ferguson S.J.;
"Escherichia coli DipZ: anatomy of a transmembrane protein disulphide
reductase in which three pairs of cysteine residues, one in each of
three domains, contribute differentially to function.";
Mol. Microbiol. 35:1360-1374(2000).
[8]
PROTEIN SEQUENCE OF 20-27, TOPOLOGY, AND MUTAGENESIS OF CYS-122;
CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483.
STRAIN=BL21-DE3;
PubMed=10712691; DOI=10.1046/j.1365-2958.2000.01778.x;
Chung J., Chen T., Missiakas D.;
"Transfer of electrons across the cytoplasmic membrane by DsbD, a
membrane protein involved in thiol-disulphide exchange and protein
folding in the bacterial periplasm.";
Mol. Microbiol. 35:1099-1109(2000).
[9]
PROTEIN SEQUENCE OF 78-82.
Missiakas D., Hughes G.J., Frutiger S., Paquet N., Raina S.;
Submitted (MAY-1995) to UniProtKB.
[10]
CHARACTERIZATION.
PubMed=7957865; DOI=10.1016/0014-5793(94)01053-6;
Sambongi Y., Ferguson S.J.;
"Specific thiol compounds complement deficiency in c-type cytochrome
biogenesis in Escherichia coli carrying a mutation in a membrane-bound
disulphide isomerase-like protein.";
FEBS Lett. 353:235-238(1994).
[11]
TOPOLOGY, AND MUTAGENESIS OF CYS-13; CYS-122; CYS-128; CYS-182;
CYS-301; CYS-304; CYS-480 AND CYS-483.
STRAIN=DHB4, and RI242;
PubMed=10545108; DOI=10.1093/emboj/18.21.5963;
Stewart E.J., Katzen F., Beckwith J.;
"Six conserved cysteines of the membrane protein DsbD are required for
the transfer of electrons from the cytoplasm to the periplasm of
Escherichia coli.";
EMBO J. 18:5963-5971(1999).
[12]
CHARACTERIZATION.
PubMed=11114333; DOI=10.1016/S0092-8674(00)00180-X;
Katzen F., Beckwith J.;
"Transmembrane electron transfer by the membrane protein DsbD occurs
via a disulfide bond cascade.";
Cell 103:769-779(2000).
[13]
CHARACTERIZATION.
STRAIN=K38;
PubMed=11085993; DOI=10.1074/jbc.M009500200;
Krupp R., Chan C., Missiakas D.;
"DsbD-catalyzed transport of electrons across the membrane of
Escherichia coli.";
J. Biol. Chem. 276:3696-3701(2001).
[14]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
-!- FUNCTION: Required to facilitate the formation of correct
disulfide bonds in some periplasmic proteins and for the assembly
of the periplasmic c-type cytochromes. Acts by transferring
electrons from cytoplasmic thioredoxin to the periplasm, thereby
maintaining the active site of DsbC, DsbE and DsbG in a reduced
state. This transfer involves a cascade of disulfide bond
formation and reduction steps.
-!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
disulfide + NAD(P)H.
-!- INTERACTION:
P0AA86:dsbE; NbExp=4; IntAct=EBI-9014057, EBI-9014059;
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- MISCELLANEOUS: The consequences of replacement of the cysteines
with alanines were found to depend on the conditions tested and on
the reporter system used for the analysis, and then differ
depending on the references.
-!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA54781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA85375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z36905; CAA85375.1; ALT_INIT; Genomic_DNA.
EMBL; X77707; CAA54781.1; ALT_INIT; Genomic_DNA.
EMBL; U14003; AAA97035.1; -; Genomic_DNA.
EMBL; U00096; AAC77096.1; -; Genomic_DNA.
EMBL; AP009048; BAE78138.1; -; Genomic_DNA.
PIR; S56364; S56364.
RefSeq; NP_418559.1; NC_000913.3.
RefSeq; WP_000068922.1; NZ_LN832404.1.
PDB; 1JPE; X-ray; 1.90 A; A=20-151.
PDB; 1JZD; X-ray; 2.30 A; C=20-151.
PDB; 1L6P; X-ray; 1.65 A; A=20-144.
PDB; 1VRS; X-ray; 2.85 A; A/B/C=20-162, D/E/F=438-565.
PDB; 1Z5Y; X-ray; 1.94 A; D=20-162.
PDB; 2FWE; X-ray; 1.65 A; A=438-565.
PDB; 2FWF; X-ray; 1.30 A; A=438-565.
PDB; 2FWG; X-ray; 1.10 A; A=438-565.
PDB; 2FWH; X-ray; 0.99 A; A=438-565.
PDB; 3PFU; X-ray; 1.80 A; A=21-151.
PDB; 4IP1; X-ray; 2.47 A; A=444-565.
PDB; 4IP6; X-ray; 2.23 A; A=444-565.
PDB; 5NHI; X-ray; 2.60 A; A/B=21-151.
PDBsum; 1JPE; -.
PDBsum; 1JZD; -.
PDBsum; 1L6P; -.
PDBsum; 1VRS; -.
PDBsum; 1Z5Y; -.
PDBsum; 2FWE; -.
PDBsum; 2FWF; -.
PDBsum; 2FWG; -.
PDBsum; 2FWH; -.
PDBsum; 3PFU; -.
PDBsum; 4IP1; -.
PDBsum; 4IP6; -.
PDBsum; 5NHI; -.
ProteinModelPortal; P36655; -.
SMR; P36655; -.
BioGrid; 4262691; 1010.
DIP; DIP-9476N; -.
IntAct; P36655; 1.
STRING; 316385.ECDH10B_4329; -.
TCDB; 5.A.1.1.1; the disulfide bond oxidoreductase d (dsbd) family.
PaxDb; P36655; -.
PRIDE; P36655; -.
EnsemblBacteria; AAC77096; AAC77096; b4136.
EnsemblBacteria; BAE78138; BAE78138; BAE78138.
GeneID; 948649; -.
KEGG; ecj:JW5734; -.
KEGG; eco:b4136; -.
PATRIC; fig|511145.12.peg.4267; -.
EchoBASE; EB2095; -.
EcoGene; EG12178; dipZ.
eggNOG; ENOG4105CSG; Bacteria.
eggNOG; COG4232; LUCA.
HOGENOM; HOG000254981; -.
InParanoid; P36655; -.
KO; K04084; -.
OMA; FVYVQGM; -.
PhylomeDB; P36655; -.
BioCyc; EcoCyc:DSBD-MONOMER; -.
BioCyc; MetaCyc:DSBD-MONOMER; -.
EvolutionaryTrace; P36655; -.
PRO; PR:P36655; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IMP:EcoCyc.
GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0045454; P:cell redox homeostasis; IMP:EcoCyc.
GO; GO:0071502; P:cellular response to temperature stimulus; IMP:EcoliWiki.
GO; GO:0017004; P:cytochrome complex assembly; IMP:EcoliWiki.
GO; GO:0055114; P:oxidation-reduction process; IDA:EcoCyc.
GO; GO:0042493; P:response to drug; IMP:EcoliWiki.
CDD; cd02953; DsbDgamma; 1.
Gene3D; 2.60.40.1250; -; 1.
HAMAP; MF_00399; DbsD; 1.
InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
InterPro; IPR035671; DsbD_gamma.
InterPro; IPR028250; DsbDN.
InterPro; IPR036929; DsbDN_sf.
InterPro; IPR022910; Thiol_diS_interchange_DbsD.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
Pfam; PF11412; DsbC; 1.
Pfam; PF02683; DsbD; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF74863; SSF74863; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Cytochrome c-type biogenesis; Direct protein sequencing;
Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
Redox-active center; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
CHAIN 20 565 Thiol:disulfide interchange protein DsbD.
/FTId=PRO_0000007373.
TOPO_DOM 20 162 Periplasmic. {ECO:0000255}.
TRANSMEM 163 183 Helical. {ECO:0000255}.
TOPO_DOM 184 207 Cytoplasmic. {ECO:0000255}.
TRANSMEM 208 228 Helical. {ECO:0000255}.
TOPO_DOM 229 242 Periplasmic. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TOPO_DOM 264 295 Cytoplasmic. {ECO:0000255}.
TRANSMEM 296 316 Helical. {ECO:0000255}.
TOPO_DOM 317 322 Periplasmic. {ECO:0000255}.
TRANSMEM 323 343 Helical. {ECO:0000255}.
TOPO_DOM 344 356 Cytoplasmic. {ECO:0000255}.
TRANSMEM 357 377 Helical. {ECO:0000255}.
TOPO_DOM 378 383 Periplasmic. {ECO:0000255}.
TRANSMEM 384 404 Helical. {ECO:0000255}.
TOPO_DOM 405 417 Cytoplasmic. {ECO:0000255}.
TRANSMEM 418 438 Helical. {ECO:0000255}.
TOPO_DOM 439 565 Periplasmic. {ECO:0000255}.
DOMAIN 434 565 Thioredoxin.
DISULFID 122 128 Redox-active. {ECO:0000305}.
DISULFID 182 304 Redox-active. {ECO:0000305}.
DISULFID 480 483 Redox-active. {ECO:0000305}.
MUTAGEN 13 13 C->A: No loss of activity.
{ECO:0000269|PubMed:10545108}.
MUTAGEN 122 122 C->A: Loss of activity.
{ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
MUTAGEN 128 128 C->A: Loss of activity.
{ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
MUTAGEN 182 182 C->A: Loss of activity.
{ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
MUTAGEN 301 301 C->A: No loss of activity.
{ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
MUTAGEN 304 304 C->A: Loss of activity.
{ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
MUTAGEN 480 480 C->A: Loss of activity; when associated
with A-483. {ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
MUTAGEN 483 483 C->A: Loss of activity; when associated
with A-480. {ECO:0000269|PubMed:10545108,
ECO:0000269|PubMed:10712691,
ECO:0000269|PubMed:10760137}.
STRAND 25 28 {ECO:0000244|PDB:1L6P}.
HELIX 33 36 {ECO:0000244|PDB:1L6P}.
STRAND 37 44 {ECO:0000244|PDB:1L6P}.
STRAND 47 54 {ECO:0000244|PDB:1L6P}.
STRAND 58 61 {ECO:0000244|PDB:1L6P}.
HELIX 62 64 {ECO:0000244|PDB:1L6P}.
STRAND 66 74 {ECO:0000244|PDB:1L6P}.
STRAND 83 87 {ECO:0000244|PDB:1L6P}.
TURN 88 90 {ECO:0000244|PDB:1L6P}.
STRAND 91 96 {ECO:0000244|PDB:1L6P}.
STRAND 98 119 {ECO:0000244|PDB:1L6P}.
STRAND 121 123 {ECO:0000244|PDB:1L6P}.
TURN 124 126 {ECO:0000244|PDB:1L6P}.
STRAND 132 137 {ECO:0000244|PDB:1L6P}.
HELIX 456 466 {ECO:0000244|PDB:2FWH}.
STRAND 471 476 {ECO:0000244|PDB:2FWH}.
HELIX 481 489 {ECO:0000244|PDB:2FWH}.
TURN 490 492 {ECO:0000244|PDB:2FWH}.
HELIX 494 499 {ECO:0000244|PDB:2FWH}.
TURN 500 502 {ECO:0000244|PDB:2FWH}.
STRAND 503 509 {ECO:0000244|PDB:2FWH}.
HELIX 515 523 {ECO:0000244|PDB:2FWH}.
STRAND 528 535 {ECO:0000244|PDB:2FWH}.
HELIX 543 545 {ECO:0000244|PDB:2FWH}.
STRAND 547 549 {ECO:0000244|PDB:1VRS}.
HELIX 553 562 {ECO:0000244|PDB:2FWH}.
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


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