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Database: UniProt
Entry: A0A0A5HVD4_9VIBR
LinkDB: A0A0A5HVD4_9VIBR
Original site: A0A0A5HVD4_9VIBR 
ID   A0A0A5HVD4_9VIBR        Unreviewed;       247 AA.
AC   A0A0A5HVD4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-APR-2018, entry version 25.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=NM06_12515 {ECO:0000313|EMBL:KGY08285.1};
OS   Vibrio sinaloensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=379097 {ECO:0000313|EMBL:KGY08285.1, ECO:0000313|Proteomes:UP000030451};
RN   [1] {ECO:0000313|EMBL:KGY08285.1, ECO:0000313|Proteomes:UP000030451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T08 {ECO:0000313|EMBL:KGY08285.1,
RC   ECO:0000313|Proteomes:UP000030451};
RA   Chan K.-G., Mohamad N.I.;
RT   "Genome sequencing of Vibrio sinaloensis T08.";
RL   Submitted (OCT-2014) 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:KGY08285.1}.
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DR   EMBL; JRWP01000026; KGY08285.1; -; Genomic_DNA.
DR   RefSeq; WP_038191314.1; NZ_JXBJ01000004.1.
DR   ProteinModelPortal; A0A0A5HVD4; -.
DR   EnsemblBacteria; KGY08285; KGY08285; NM06_12515.
DR   Proteomes; UP000030451; Unassembled WGS sequence.
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:UP000030451};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030451};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     23       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        24    247       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010001197.
FT   DOMAIN       30     84       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      116    244       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   247 AA;  27189 MW;  EFD0F34DCE109CF1 CRC64;
     MSVLRRMTLL TLPLLLAAQS VSANEVTFDK AQLEARFAKL GLEVKQVVPA DIDGLVEVQT
     TGGVLFASPT GDYFLAGTLY KLDGNGQYED VLAKRQAPIN AAKIESFKDS MIEFKADNEK
     YVVTVFTDIT CGYCVRLHNQ MQGYNELGIT VRYMAYPRQG GTGSVADQMA AIWGAENPQS
     AMHDGKVNRK FPEQSKDFAK YQDIIKQHYA LGRELGISGT PAIFLPNGEM VGGYLPPAQL
     LQRLEQI
//
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