(data stored in SCRATCH zone)

SWISSPROT: Q3IDT3_PSEHT

ID   Q3IDT3_PSEHT            Unreviewed;       603 AA.
AC   Q3IDT3;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 101.
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};
DE   Flags: Precursor;
GN   Name=dipZ {ECO:0000313|EMBL:CAI85362.1};
GN   Synonyms=dsbD {ECO:0000256|HAMAP-Rule:MF_00399};
GN   OrderedLocusNames=PSHAa0263 {ECO:0000313|EMBL:CAI85362.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85362.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85362.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}.
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DR   EMBL; CR954246; CAI85362.1; -; Genomic_DNA.
DR   RefSeq; WP_011326976.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDT3; -.
DR   STRING; 326442.PSHAa0263; -.
DR   EnsemblBacteria; CAI85362; CAI85362; PSHAa0263.
DR   KEGG; pha:PSHAa0263; -.
DR   PATRIC; fig|326442.8.peg.250; -.
DR   eggNOG; ENOG4105CSG; Bacteria.
DR   eggNOG; COG4232; LUCA.
DR   HOGENOM; HOG000254981; -.
DR   KO; K04084; -.
DR   OMA; FVYVQGM; -.
DR   OrthoDB; POG091H0F5X; -.
DR   Proteomes; UP000006843; Chromosome I.
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; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF4; PTHR32234:SF4; 1.
DR   Pfam; PF11412; DsbC; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF74863; SSF74863; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IDT3.
DR   SWISS-2DPAGE; Q3IDT3.
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:UP000006843};
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:CAI85362.1};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
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   SIGNAL        1     18       {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   CHAIN        19    603       Thiol:disulfide interchange protein DsbD.
FT                                {ECO:0000256|HAMAP-Rule:MF_00399}.
FT                                /FTId=PRO_5009019146.
FT   TRANSMEM    198    225       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    237    261       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    273    293       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    314    332       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    352    373       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    394    410       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    416    434       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    446    467       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DOMAIN      467    600       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID    125    131       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    515    518       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
SQ   SEQUENCE   603 AA;  65708 MW;  DF2214508618C92B CRC64;
     MRFFFLLLVA LLAAPAKANN ILGDLLAPPQ QTFLQVDQAF VFDFDQQDNT LFIGWDIAPE
     YYLYKNKIEI IAKGANIEVG DLGNGEVIED EFFGKTEVFF NALSIVSKLS NVTEGAVVKV
     RYQGCAEAGL CYPPEVISIP LNKIAGEQLQ NADDATHSAT SANAFTALSQ ANAPTSNAPK
     KDLTFTEQLA SQGLITNLLI FFVVGVGLAF TPCVFPMFPI LSSLIAGQKN LSTKKAFALS
     FVYIQGMAVT YAALGLVVAA LGGQVQGYLQ HPYVLISFSL LFVLLAMSMF GWYEIKLPSG
     MMNKLTQVSN NQKGGNYVGV FLMGVLSGLI ASPCTTAPLS AALLFVAQSG DYLVGGLTLY
     VLSLGMGLPL LLLGTSGGKL LPKAGGWMEQ VKTLFGFIML VVPLILLERL LDADVILLMA
     GVLALATALY LHHWQSSQTQ GKLKTALWFA ATLLVVSGFN LTKNYFWPVH MQTMQVSAQS
     NEFKQVANLT ELKAAVAHAN EQGRLVMVDL YADWCIACKE FEHYTFPDAK VQNEFSHFEL
     IQVDLTDSDN KTIELMEEYT VFGLPSILFF NTQGEELSAQ RVTGFLNAED FAQHLSTVRA
     SVK
//

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