(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NPL9_YERPA

ID   A0A0E1NPL9_YERPA        Unreviewed;       238 AA.
AC   A0A0E1NPL9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 22.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
DE   Flags: Precursor;
GN   OrderedLocusNames=YPA_0378 {ECO:0000313|EMBL:ABG12346.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12346.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12346.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12346.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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}.
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DR   EMBL; CP000308; ABG12346.1; -; Genomic_DNA.
DR   RefSeq; WP_002209932.1; NZ_CP009906.1.
DR   SMR; A0A0E1NPL9; -.
DR   EnsemblBacteria; ABG12346; ABG12346; YPA_0378.
DR   EnsemblBacteria; AJJ78187; AJJ78187; CH58_3224.
DR   KEGG; ypa:YPA_0378; -.
DR   PATRIC; fig|360102.15.peg.3386; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   BioCyc; YPES360102:GHZU-398-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
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;
DR   PRODOM; A0A0E1NPL9.
DR   SWISS-2DPAGE; A0A0E1NPL9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        22    238       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5009994133.
SQ   SEQUENCE   238 AA;  25997 MW;  FBF93E6B8D1F50AD CRC64;
     MKKSLLLLPM LMAALSGVAN ADDSAIQQTL KKLDIQQADI QPSPIPGIST VMTESGVLYI
     SADGKHLLQG PLYDVSGDQP INVTNQALLK KLEALSSEMI VYKAPEEKHV ITVFTDITCG
     YCRKLHEQMK DYNALGITVR YLAFPRQGLS SQAEKDMRSI WCMADRNKAF DDAMKNNDIS
     PATCKTDISK HYQLGVQFGI QGTPAIVLQN GTIVPGYQGP KEMLQMLNAH QASLKAGG
//

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