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Database: UniProt
Entry: A0A0Q5DRJ6_9BURK
LinkDB: A0A0Q5DRJ6_9BURK
Original site: A0A0Q5DRJ6_9BURK 
ID   A0A0Q5DRJ6_9BURK        Unreviewed;       315 AA.
AC   A0A0Q5DRJ6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-APR-2018, entry version 12.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=ASF61_21340 {ECO:0000313|EMBL:KQQ44675.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ44675.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ44675.1, ECO:0000313|Proteomes:UP000051032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ44675.1,
RC   ECO:0000313|Proteomes:UP000051032};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ44675.1, ECO:0000313|Proteomes:UP000051032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ44675.1,
RC   ECO:0000313|Proteomes:UP000051032};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQQ44675.1}.
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DR   EMBL; LMNW01000006; KQQ44675.1; -; Genomic_DNA.
DR   EnsemblBacteria; KQQ44675; KQQ44675; ASF61_21340.
DR   Proteomes; UP000051032; 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; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000051032};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051032};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     28       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        29    315       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010005557.
FT   DOMAIN       91    143       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      181    312       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   315 AA;  33105 MW;  A0DC0393A4109357 CRC64;
     MSTLNTNSTR ARVLLTMAAL LASCGAAGDA PDCAAGAAQD YAVAAAPDYA ASAAQDDATG
     AAAAALHAAH ADPAKAAEKV DTAETAEAAM RQLLAQRYPS TTFGAIARTP VPGLWEVWMG
     SNVAYMTDEG RHFIFGHLYD MQTQTDLTAA SKNATLRQDQ PDRPRLAFQE LPLADAIKTV
     RGSGARQLAV FSDPHCPYCR QLEQELAKLD NVTIYTFLFP LASLHPQATA VAQAIWCQAD
     RAVAWRDFNQ TGKPPKSAKP AKSLSSIACS TPIARNVALA ERSGISGTPY ILFANGGSAA
     GAMSAAELEA RLARP
//
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