(data stored in SCRATCH9089 zone)

SWISSPROT: DSBC_PASMU

ID   DSBC_PASMU              Reviewed;         227 AA.
AC   Q9CP65;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Thiol:disulfide interchange protein DsbC;
DE   Flags: Precursor;
GN   Name=dsbC; OrderedLocusNames=PM0191;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by transferring its disulfide bond to other proteins and
CC       is reduced in the process. DsbC is reoxidized by a yet uncharacterized
CC       protein. Also acts as a disulfide isomerase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000305}.
DR   EMBL; AE004439; AAK02275.1; -; Genomic_DNA.
DR   RefSeq; WP_005756009.1; NC_002663.1.
DR   SMR; Q9CP65; -.
DR   EnsemblBacteria; AAK02275; AAK02275; PM0191.
DR   GeneID; 29388415; -.
DR   KEGG; pmu:PM0191; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   HOGENOM; HOG000222077; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   BioCyc; PMUL272843:G1FZ8-199-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   Gene3D; 3.40.30.10; -; 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   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CP65.
DR   SWISS-2DPAGE; Q9CP65.
KW   Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..227
FT                   /note="Thiol:disulfide interchange protein DsbC"
FT                   /id="PRO_0000034277"
FT   DISULFID        117..120
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   227 AA;  25029 MW;  EBED83CA26264B9C CRC64;
     MKKILSTLLM LGMSSLTFAN SQQVVEQLQK MGLSGVEVSD SPVKGIKTAV TDNGIFYITE
     DAKYILDGKL YALSEKGLRD VSSSLLLDKL TAYKNEMVVY PAKDEKHVIT VFMDTSCHYC
     KVLHKQIKEY NDLGITVRYL AFPRGGVQSK TAREMEAIFT AQDPQFALTE AINGNPPKTL
     KDANITKKHY QLGLQFGVNG TPSIVTEKGE LIGGYLKPAD LLSELAQ
//

If you have problems or comments...

PBIL Back to PBIL home page