DSBD_CAMJE
ID DSBD_CAMJE Reviewed; 567 AA.
AC Q9PHR3; Q0PAR4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=Cj0603c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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; AL111168; CAL34749.1; -; Genomic_DNA.
DR PIR; B81408; B81408.
DR RefSeq; WP_002852245.1; NC_002163.1.
DR RefSeq; YP_002344033.1; NC_002163.1.
DR AlphaFoldDB; Q9PHR3; -.
DR SMR; Q9PHR3; -.
DR IntAct; Q9PHR3; 3.
DR STRING; 192222.Cj0603c; -.
DR PaxDb; Q9PHR3; -.
DR PRIDE; Q9PHR3; -.
DR EnsemblBacteria; CAL34749; CAL34749; Cj0603c.
DR GeneID; 904931; -.
DR KEGG; cje:Cj0603c; -.
DR PATRIC; fig|192222.6.peg.595; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_0_7; -.
DR OMA; CKEMERF; -.
DR Proteomes; UP000000799; 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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..567
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007372"
FT TOPO_DOM 17..166
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..247
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..332
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..385
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..567
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 430..567
FT /note="Thioredoxin"
FT DISULFID 111..117
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 186..307
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 488..491
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 567 AA; 63786 MW; CBEE897144D24852 CRC64;
MRIFGIILLS FCLCFASILS LNEAFNVKSN SYNNSISIDI ELGKDIYLYS NKLKLYINEK
DISSLINLPQ SSTRGNENVY YQKLNLALPN LLLERFAKNT TNLIKLEFQG CSEQGLCYNP
QTWYFDLISK KDAFEISKPY KAQKTDKKTK IESEESSIAN FLATDNFFWI LLSFFGYGLL
LSLTPCILPM IPILSSLIVA KSNAKFSKKY SFFLSFIYVF FMSLAYAIAG VIASFLGASI
QGILQKPIIL ILFALIFIAF AFAMFGAFRF ELPLRFQTFI HKKSEKGKGV VGIAIMGFLS
ALIVGPCVAA PLAGALIYIA NTGNALLGGS ALFIMSFGMG IPLLFIGLGL GFIKPGFWME
KVKIFFGFVM LAMAIWILSR IIEENYILIA YGILGVFFSV FMGIFEKSFT IISKIKKSIL
ILILAYSLSI FLGGLFGAKN FLNPLNFNTI SASKHALSYD YINNFEQLKQ EIQTNTKPIM
LDFTASWCEN CKLLDELTFS DERIIQKMQN YKLIKVDVSE NNNEQIKTMK EFNVFGPPVL
IFFENGKEKL KITGFISADD LLKKIEP
