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Database: UniProt
Entry: A3WDC5_9SPHN
LinkDB: A3WDC5_9SPHN
Original site: A3WDC5_9SPHN 
ID   A3WDC5_9SPHN            Unreviewed;       292 AA.
AC   A3WDC5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   25-APR-2018, entry version 47.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=NAP1_03440 {ECO:0000313|EMBL:EAQ29794.1};
OS   Erythrobacter sp. NAP1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ29794.1, ECO:0000313|Proteomes:UP000002995};
RN   [1] {ECO:0000313|EMBL:EAQ29794.1, ECO:0000313|Proteomes:UP000002995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAP1 {ECO:0000313|EMBL:EAQ29794.1,
RC   ECO:0000313|Proteomes:UP000002995};
RX   PubMed=21952547; DOI=10.1128/JB.05845-11;
RA   Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA   Falkowski P.G.;
RT   "Genome Sequence of the Marine Photoheterotrophic Bacterium
RT   Erythrobacter sp. Strain NAP1.";
RL   J. Bacteriol. 193:5881-5882(2011).
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:EAQ29794.1}.
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DR   EMBL; AAMW01000001; EAQ29794.1; -; Genomic_DNA.
DR   RefSeq; WP_007163824.1; NZ_CH672390.1.
DR   ProteinModelPortal; A3WDC5; -.
DR   STRING; 237727.NAP1_03440; -.
DR   EnsemblBacteria; EAQ29794; EAQ29794; NAP1_03440.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   OrthoDB; POG091H04JN; -.
DR   Proteomes; UP000002995; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 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:UP000002995};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002995};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     42       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        43    292       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010004537.
FT   DOMAIN       50    102       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      165    282       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   292 AA;  31007 MW;  E4F582F7521C3B41 CRC64;
     MNYSNQRPGL KARAAHISLA AASAAALLTS GVAVVTAMPA QAAITQNVVE ALKLRLPKTP
     IDALDCKTFA PWCEVVSGET LFYIDEAARY LFVGRLYDME ERRDVTAARL LELNPDLLAA
     GAARAAGEDT AGRHDVAEPR DRRAATHVDL KVLPAVGAIL WGNPKGPKLV VFSDFQCGYC
     KRLTGELEKA GVLVEERPIS IFGASSRRMS EAVLCAADPV GALHAAYTGK HLEPRAACKK
     AAALDANEAF AQANGFAGTP VIVRARDGAV LHGYRDAKTL RAFANAKTGS KQ
//
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