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Database: UniProt
Entry: A1TKJ4_ACIAC
LinkDB: A1TKJ4_ACIAC
Original site: A1TKJ4_ACIAC 
ID   A1TKJ4_ACIAC            Unreviewed;       246 AA.
AC   A1TKJ4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   25-APR-2018, entry version 72.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   OrderedLocusNames=Aave_0884 {ECO:0000313|EMBL:ABM31482.1};
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp.
OS   citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945 {ECO:0000313|EMBL:ABM31482.1, ECO:0000313|Proteomes:UP000002596};
RN   [1] {ECO:0000313|EMBL:ABM31482.1, ECO:0000313|Proteomes:UP000002596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1 {ECO:0000313|EMBL:ABM31482.1,
RC   ECO:0000313|Proteomes:UP000002596};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D.,
RA   Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1 {ECO:0000313|Proteomes:UP000002596};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D.,
RA   Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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}.
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DR   EMBL; CP000512; ABM31482.1; -; Genomic_DNA.
DR   RefSeq; WP_011794040.1; NC_008752.1.
DR   ProteinModelPortal; A1TKJ4; -.
DR   STRING; 397945.Aave_0884; -.
DR   EnsemblBacteria; ABM31482; ABM31482; Aave_0884.
DR   KEGG; aav:Aave_0884; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   HOGENOM; HOG000222078; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; ACIT397945:G1G7T-889-MONOMER; -.
DR   Proteomes; UP000002596; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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   InterPro; IPR017937; Thioredoxin_CS.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002596};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002596};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     22       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        23    246       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010001116.
FT   DOMAIN       28     82       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      111    232       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   246 AA;  26808 MW;  A9D7A17261994FA9 CRC64;
     MKLIPALLAG AAALTLGLGA HAQESAIRKA LGSRIPQLQN IDEVRATPMQ GLYEVRIGTD
     VFYTDAKGNY LIQGELIDTK ARRNLTEDRI NKLTAVDFAS LPFQDAFTIV RGNGQRKLAV
     FEDPNCGYCK RFEKDLQNVD NVTVYLFLYP ILSPDSAEKS RNIWCSKDRA AAWQDHMVRD
     KTTPAASCDT AAVQRNLAFG KKHKITGTPT LIFTDGSRVP GAIDAREVEK RLADAGSGAG
     PAPATN
//
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