DSBD_NEIMA
ID DSBD_NEIMA Reviewed; 601 AA.
AC Q9JTL9; A1IST6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=NMA1719;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM08848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL157959; CAM08848.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9JTL9; -.
DR BMRB; Q9JTL9; -.
DR SASBDB; Q9JTL9; -.
DR SMR; Q9JTL9; -.
DR TCDB; 5.A.1.1.2; the disulfide bond oxidoreductase d (dsbd) family.
DR EnsemblBacteria; CAM08848; CAM08848; NMA1719.
DR KEGG; nma:NMA1719; -.
DR HOGENOM; CLU_014657_3_0_4; -.
DR BioCyc; NMEN122587:NMA_RS08675-MON; -.
DR Proteomes; UP000000626; 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: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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
KW Redox-active center; Signal; 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_0000007377"
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..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..601
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 467..601
FT /note="Thioredoxin"
FT REGION 137..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"
SQ SEQUENCE 601 AA; 64865 MW; 22FE36062AD5C78E CRC64;
MKKLICLFAV FLMLCGRAFA LDANDLLPPE KAFVPELAVA DDGVNVRFRI ADGYYMYQAK
IVGKTDPADL LGQPSFSKGE EKEDEFFGRQ TVYHHEAQVA FPYAKAVGEP YKLVLTYQGC
AEAGVCYPPV DTEFDISGNG TYHPQTDEPA SAKDRFLQPS SQNGSGALPP PKGDEGGDSR
FKLSWDTLNA NLLAFFLAGL GLSFTACMYP LLPIVSSIVV GDKKAGKARA FVLSVVYVQG
LSLTYTLVGI VAGLTGALLT VWLQQAWVVL AASALMVVLA LSMFGLFNIQ LPNAVQSYFQ
NQSSRLSGGK IVSVFIMGIL SALIVGPCVA PPLAFALGYI GQTGDAVLGG LALYTLALGT
GVPLIAIGTF GGHILPRAGD WMNAVKYAFG FILLAVAVYL ATPHLPYYLV VALYTLLMLV
PACMLLVNGR RQKRRPKAVA FALGGILLIG GAWFGWQGAN GKTTALHHFL TLNPPAEAGK
SSEHGKMFAD TAALKAAMDT ALKEHPDKPV VLDFYADWCI SCKEMAAYTL NQPEVHQAVD
MERFFQIDVT ANTPEHQALL KEYGLFGPPG VFVVRSDGSR SEPLLGFVKA DKFIEWYEQN
R
