(data stored in SCRATCH zone)

SWISSPROT: C5BDJ9_EDWI9

ID   C5BDJ9_EDWI9            Unreviewed;       575 AA.
AC   C5BDJ9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 61.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000256|HAMAP-Rule:MF_00399};
DE            EC=1.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00399};
DE   AltName: Full=Protein-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE            Short=Disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
GN   Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399};
GN   OrderedLocusNames=NT01EI_0374 {ECO:0000313|EMBL:ACR67615.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67615.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required to facilitate the formation of correct
CC       disulfide bonds in some periplasmic proteins and for the assembly
CC       of the periplasmic c-type cytochromes. Acts by transferring
CC       electrons from cytoplasmic thioredoxin to the periplasm. This
CC       transfer involves a cascade of disulfide bond formation and
CC       reduction steps. {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00399}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00399}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00399}.
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DR   EMBL; CP001600; ACR67615.1; -; Genomic_DNA.
DR   RefSeq; WP_015869821.1; NC_012779.2.
DR   ProteinModelPortal; C5BDJ9; -.
DR   STRING; 634503.NT01EI_0374; -.
DR   EnsemblBacteria; ACR67615; ACR67615; NT01EI_0374.
DR   GeneID; 7960154; -.
DR   KEGG; eic:NT01EI_0374; -.
DR   PATRIC; fig|634503.3.peg.338; -.
DR   eggNOG; ENOG4105CSG; Bacteria.
DR   eggNOG; COG4232; LUCA.
DR   HOGENOM; HOG000254981; -.
DR   KO; K04084; -.
DR   OMA; FVYVQGM; -.
DR   OrthoDB; POG091H0F5X; -.
DR   Proteomes; UP000001485; 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 carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-HAMAP.
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; IPR022910; Thiol_diS_interchange_DbsD.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF4; PTHR32234:SF4; 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   3: Inferred from homology;
DR   PRODOM; C5BDJ9.
DR   SWISS-2DPAGE; C5BDJ9.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytochrome c-type biogenesis {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093715};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000313|EMBL:ACR67615.1};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00464121};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093729};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   TRANSMEM    171    199       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    211    235       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    247    269       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    290    321       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    333    355       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    367    385       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    391    410       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DOMAIN      446    573       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID    122    128       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    186    308       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    488    491       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
SQ   SEQUENCE   575 AA;  62839 MW;  AFA49750A527861C CRC64;
     MAQRIFALIA LFITTLLPAQ ASLFGGQPRF VPVNQAFAFD FQQRGESLTL RWQIQPGYYL
     YRQQIRITPH QAQLGHWQLP PGIPHHDEFQ GETAIFRDGL SLTLPLLSAA AGGEVSVTYQ
     GCAAAGFCYP PETRRIPLKA ITAAVGVLPP PGTAAMATAN TEHAPTLPFP ALWALLIGIG
     IAFTPCVLPM YPLISALILG QKQRHGWGHT ALLALVYVQG MAITYTVLGM VVAAAGLRFQ
     AAFQHPYVLI GLSLLFILLA LSMFGAFTLQ LPASLQTRLT LWSNRQRSGS LLGVFVMGAL
     AGLICSPCTT APLSAILLYI AQNGNLWVGG GTLYLYALGM GIPLIAVTLF GNRLLPRSGP
     WMQHVKEGFG FVILALPVFL LERILGDAWG ARLWSLLGIT FFLWGFSLSL HARRRGTRLW
     QILLLGAALI CARPLQDWIF DETPRASIGV SAPLAFQPID SPQQLTQALA QAKARRQPVM
     LDFYADWCTA CKEFEKYTFS NDAVRSQLAG TLLLQANVTA NTEQHAQLLQ QLNVLGLPSI
     LFFTPDGQPL DDARVTGFMD AKRFLAHLQQ LPYAQ
//

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