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Database: UniProt
Entry: S6BM76_PSERE
LinkDB: S6BM76_PSERE
Original site: S6BM76_PSERE 
ID   S6BM76_PSERE            Unreviewed;       242 AA.
AC   S6BM76;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-APR-2018, entry version 25.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbC {ECO:0000313|EMBL:BAN50354.1};
GN   ORFNames=PCA10_46220 {ECO:0000313|EMBL:BAN50354.1};
OS   Pseudomonas resinovorans NBRC 106553.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50354.1, ECO:0000313|Proteomes:UP000015503};
RN   [1] {ECO:0000313|EMBL:BAN50354.1, ECO:0000313|Proteomes:UP000015503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50354.1};
RA   Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H.,
RA   Yamazoe A., Fujita N., Nojiri H.;
RT   "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT   resinovorans Strain CA10 (NBRC 106553).";
RL   Genome Announc. 1:e00488-13(2013).
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; AP013068; BAN50354.1; -; Genomic_DNA.
DR   RefSeq; WP_016494483.1; NC_021499.1.
DR   EnsemblBacteria; BAN50354; BAN50354; PCA10_46220.
DR   KEGG; pre:PCA10_46220; -.
DR   PATRIC; fig|1245471.3.peg.4677; -.
DR   KO; K03981; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; PRES1245471:G1HI7-4641-MONOMER; -.
DR   Proteomes; UP000015503; 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   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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000015503};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015503};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        22    242       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010003619.
FT   DOMAIN       29     82       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      118    237       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   242 AA;  26214 MW;  7E798DDBCF03CE62 CRC64;
     MRVTRLIAGL ALGLASTISL ADDPDQAIRK TLDALQLGLP IESIGESPMS GIYQVQLKGG
     RMLYTSADGQ YLMQGYLYHV KDGKPVNLTE QAESRSIAKE INAVPTSEMV VFSPKEPAKA
     HITVFTDTDC GYCQKLHSEV PELNRRGIEV RYMAFPRQGI GSHGYNSLVS VWCSKDRQAA
     MDKAKSREEL PPATCANPVA KQFELGQLIG VNGTPAIVLG NGQMIPGYQP APQLAKIALE
     AK
//
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