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Database: UniProt
Entry: W1DM17_KLEPN
LinkDB: W1DM17_KLEPN
Original site: W1DM17_KLEPN 
ID   W1DM17_KLEPN            Unreviewed;       237 AA.
AC   W1DM17;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-APR-2018, entry version 21.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
OS   Klebsiella pneumoniae IS43.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL09760.1, ECO:0000313|Proteomes:UP000019183};
RN   [1] {ECO:0000313|EMBL:CDL09760.1, ECO:0000313|Proteomes:UP000019183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS43 {ECO:0000313|EMBL:CDL09760.1,
RC   ECO:0000313|Proteomes:UP000019183};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C.,
RA   Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the
RT   General Hospital Vienna.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDL09760.1}.
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DR   EMBL; CBWK010000401; CDL09760.1; -; Genomic_DNA.
DR   ProteinModelPortal; W1DM17; -.
DR   EnsemblBacteria; CDL09760; CDL09760; CDL09760.
DR   Proteomes; UP000019183; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019183};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019183};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        22    237       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010000281.
FT   DOMAIN       27     76       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      105    227       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   237 AA;  25426 MW;  E383AF56C9F58202 CRC64;
     MKKGLLMFTL LAASLSGAAH ADSAAIKQSL AKLGVQSTDI QPSPVSGMST VLTDSGVLYV
     TDDGKHIIQG PMYDVSGAQP VNVTNQLLLG KLNALSNEMI VYKAPKEQHV ITVFTDITCG
     YCHKLHEQMS DYNALGITVR YLAFPRQGLQ SQAEQDMKAI WCAKDRNKAL DDAMNGKGVQ
     PASCSVDIAK HYTLGVQMGV NGTPAMVLSN GMVLPGYQGP KELKAFLDEH KKQTSGN
//
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