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Database: UniProt
Entry: A0A060BI56_9GAMM
LinkDB: A0A060BI56_9GAMM
Original site: A0A060BI56_9GAMM 
ID   A0A060BI56_9GAMM        Unreviewed;       259 AA.
AC   A0A060BI56;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   22-NOV-2017, entry version 19.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=FF32_18760 {ECO:0000313|EMBL:AIA76811.1};
OS   Halomonas campaniensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=213554 {ECO:0000313|EMBL:AIA76811.1, ECO:0000313|Proteomes:UP000027249};
RN   [1] {ECO:0000313|EMBL:AIA76811.1, ECO:0000313|Proteomes:UP000027249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS21 {ECO:0000313|EMBL:AIA76811.1,
RC   ECO:0000313|Proteomes:UP000027249};
RA   Haitao Y., Guo-Qiang C.;
RT   "A Seawater Based Open and Continuous Process for
RT   Polyhydroxyalkanoates Production by Recombinant Halomonas campaniensis
RT   LS21 Grown in Mixed Substrates.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP007757; AIA76811.1; -; Genomic_DNA.
DR   RefSeq; WP_038486086.1; NZ_CP007757.1.
DR   ProteinModelPortal; A0A060BI56; -.
DR   EnsemblBacteria; AIA76811; AIA76811; FF32_18760.
DR   GeneID; 32425929; -.
DR   KEGG; hcs:FF32_18760; -.
DR   KO; K03805; -.
DR   Proteomes; UP000027249; Chromosome.
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; IPR009094; DiS-bond_isomerase_DsbC_N.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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:UP000027249};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027249};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     26       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        27    259       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010005220.
FT   DOMAIN      121    253       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   259 AA;  28347 MW;  E8C2977EE58621AF CRC64;
     MKHFSLSRLS TLLLLTSIGN ISTSYAEELP APVQALTNQG ITIHGQFEAP GGMRGYGASV
     QGQELAIYLT PDGQHTIIGT LMDDQGNDLT EAQIEEHVRV PLEAQTWALL EESHWIQDGD
     ENAPRVIYTF TDANCPYCRQ LWQQSRPWVE AGEVQLRHIM VGILAPNSPA LAATLLGADD
     PAAALHDHSN GDSLSASAQP RDIEEQVYAN NQLFEELGLY ATPTSAFQRE TDSGNLRIDR
     IQGLPSEERL IEMMGGEAP
//
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