DSBD_NEIMB
ID DSBD_NEIMB Reviewed; 601 AA.
AC Q9JYM0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Thiol:disulfide interchange protein DsbD;
DE EC=1.8.1.8;
DE AltName: Full=Protein-disulfide reductase;
DE Short=Disulfide reductase;
DE Flags: Precursor;
GN Name=dsbD; OrderedLocusNames=NMB1519;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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. This transfer involves a
CC cascade of disulfide bond formation and reduction steps (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF41875.1; -; Genomic_DNA.
DR PIR; F81074; F81074.
DR RefSeq; NP_274527.1; NC_003112.2.
DR RefSeq; WP_002244193.1; NC_003112.2.
DR PDB; 2K0R; NMR; -; A=20-146.
DR PDB; 2K9F; NMR; -; B=20-146.
DR PDB; 6DNL; X-ray; 1.70 A; A=487-601.
DR PDBsum; 2K0R; -.
DR PDBsum; 2K9F; -.
DR PDBsum; 6DNL; -.
DR AlphaFoldDB; Q9JYM0; -.
DR BMRB; Q9JYM0; -.
DR SMR; Q9JYM0; -.
DR STRING; 122586.NMB1519; -.
DR PaxDb; Q9JYM0; -.
DR EnsemblBacteria; AAF41875; AAF41875; NMB1519.
DR KEGG; nme:NMB1519; -.
DR PATRIC; fig|122586.8.peg.1927; -.
DR HOGENOM; CLU_014657_3_0_4; -.
DR OMA; CKEMERF; -.
DR EvolutionaryTrace; Q9JYM0; -.
DR Proteomes; UP000000425; 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:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
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; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
DR Pfam; PF11412; DsbC; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF74863; SSF74863; 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; Disulfide bond; Electron transport; Membrane;
KW NAD; Oxidoreductase; Redox-active center; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..601
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007378"
FT TOPO_DOM 21..191
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..266
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..346
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..406
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..601
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 467..601
FT /note="Thioredoxin"
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 120..126
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 207..328
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 519..522
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2K0R"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2K0R"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2K0R"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:2K0R"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2K0R"
FT HELIX 491..504
FT /evidence="ECO:0007829|PDB:6DNL"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:6DNL"
FT HELIX 520..528
FT /evidence="ECO:0007829|PDB:6DNL"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:6DNL"
FT HELIX 533..539
FT /evidence="ECO:0007829|PDB:6DNL"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:6DNL"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:6DNL"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:6DNL"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:6DNL"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:6DNL"
FT HELIX 590..599
FT /evidence="ECO:0007829|PDB:6DNL"
SQ SEQUENCE 601 AA; 64925 MW; AC19CBBF9E763A04 CRC64;
MKKLICLFAV FLMLCGRAFA LDANDLLPPE KAFVPELAVA DDGVNVRFRI ADGYYMYQAK
IVGKTDPADL LGQPSFSKGE EKEDEFFGRQ TVYHHEAQVA FPYAKAVGEP YKLVLTYQGC
AEAGVCYPPV DTEFDIFGNG TYHPQTDEPA SAKDRFLQPS SQNGSGALPP PKGDEGGDSR
FKLSWDTLNA NLLAFFLAGL GLSFTACMYP LLPIVSSIVV GDKKAGKARA FVLSVVYVQG
LALTYTLVGI VAGLTGALLT VWLQQAWVVL AASALMVVLA LSMFGLFNIQ LPNAVQSYFQ
NQSSRLSGGK IVSVFIMGIL SALIVGPCVA PPLAFALGYI GQTGDAVLGG LALYTLALGT
GVPLIAIGTF GGHILPKAGD WMNAVKYAFG FILLAVAVYL ATPHLPYYLV VALYTLLMLV
PAFMLLVNGR RQKRRPKAVA FALGGILLIG GAWFGWQGAN GKTTALHHFL TLNPPAEAGK
SSEHGKMFAD TAALKAAMDT ALKEHPDKPV VLDFYADWCI SCKEMAAYTL NQPEVHQAVD
MERFFQIDVT ANTPEHQALL KEYGLFGPPG VFVVRSDGSR SEPLLGFVKA DKFIEWYEQN
R
