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Database: UniProt
Entry: A0A0W8JJD4_9VIBR
LinkDB: A0A0W8JJD4_9VIBR
Original site: A0A0W8JJD4_9VIBR 
ID   A0A0W8JJD4_9VIBR        Unreviewed;       244 AA.
AC   A0A0W8JJD4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-APR-2018, entry version 11.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=VRK_04740 {ECO:0000313|EMBL:KUJ00343.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUJ00343.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUJ00343.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUJ00343.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-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:KUJ00343.1}.
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DR   EMBL; LQIY01000003; KUJ00343.1; -; Genomic_DNA.
DR   RefSeq; WP_059119913.1; NZ_KQ947475.1.
DR   EnsemblBacteria; KUJ00343; KUJ00343; VRK_04740.
DR   PATRIC; fig|1761910.3.peg.475; -.
DR   Proteomes; UP000054473; 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:UP000054473};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054473};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        22    244       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010008640.
FT   DOMAIN       27     81       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      113    241       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   244 AA;  26930 MW;  BEC3F541832A7A51 CRC64;
     MRAIRELVLL GLVFFSLAAS AADSFDKQAL MQRFQSLGLS VKDVVSADVD GLVEVQTTNG
     VLFASPKGDY FIAGTLYKMK GNGQYEDVIA KRQAPINAKR IEQLKDQMIV YKADHEKYVV
     TVFTDITCGY CIRLHSQLKA YNDLGITIRY LAFPRQGPTG QVAEQMAAIW CDADPAKALN
     DAKINRDIPK PEGDISKCKK EVANHYQLGR ELGISGTPAI FLPNGEMIGG YLPPDKLLER
     LEAI
//
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