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Database: UniProt
Entry: A0A0K8P101_IDESA
LinkDB: A0A0K8P101_IDESA
Original site: A0A0K8P101_IDESA 
ID   A0A0K8P101_IDESA        Unreviewed;       247 AA.
AC   A0A0K8P101;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-APR-2018, entry version 13.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=ISF6_2151 {ECO:0000313|EMBL:GAP36311.1};
OS   Ideonella sakaiensis (strain 201-F6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Ideonella.
OX   NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP36311.1, ECO:0000313|Proteomes:UP000037660};
RN   [1] {ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=201-F6 {ECO:0000313|Proteomes:UP000037660};
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "Discovery of a poly(ethylene terephthalate assimilation.";
RL   Submitted (JUL-2015) 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:GAP36311.1}.
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DR   EMBL; BBYR01000034; GAP36311.1; -; Genomic_DNA.
DR   RefSeq; WP_054020317.1; NZ_BBYR01000034.1.
DR   EnsemblBacteria; GAP36311; GAP36311; ISF6_2151.
DR   Proteomes; UP000037660; Unassembled WGS sequence.
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:UP000037660};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037660};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     28       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        29    247       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010000918.
FT   DOMAIN       34     88       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      117    238       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   247 AA;  27159 MW;  878A5DF6627CFC58 CRC64;
     MTRSSWRPST RALCAAALLL AAVLPATAQE AVIRKNIAER LPDFPRIDEV AKTPIPGLYE
     LRIGSQIFYS DEQGNYLIEG VLVETRTKTN LTEERLSRLT AIDPATLPMK DAIVWKQGNG
     SRKLVVFADP NCGYCKRFER DLMQVKDVTV YTFLYPILGP DSNDKSRAIW CAKDSTKAWR
     DWMVDGVAPP KAAGDCDASA LQRNVALGRK HAVNGTPALI FEDGKRVPGV MAPAALERQL
     GASRSKG
//
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