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Database: UniProt
Entry: A0A172YKS8_9GAMM
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ID   A0A172YKS8_9GAMM        Unreviewed;       227 AA.
AC   A0A172YKS8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   25-APR-2018, entry version 10.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=A5892_18875 {ECO:0000313|EMBL:ANF59786.1};
OS   Halotalea alkalilenta.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halotalea.
OX   NCBI_TaxID=376489 {ECO:0000313|EMBL:ANF59786.1, ECO:0000313|Proteomes:UP000077875};
RN   [1] {ECO:0000313|EMBL:ANF59786.1, ECO:0000313|Proteomes:UP000077875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHB B 13600 {ECO:0000313|EMBL:ANF59786.1,
RC   ECO:0000313|Proteomes:UP000077875};
RA   Swarnkar M.K., Sharma A., Kaushal K., Soni R., Rana S., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequence of Halotalea alkalilenta IHB B 13600.";
RL   Submitted (APR-2016) 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; CP015243; ANF59786.1; -; Genomic_DNA.
DR   RefSeq; WP_064124631.1; NZ_CP015243.1.
DR   EnsemblBacteria; ANF59786; ANF59786; A5892_18875.
DR   KEGG; haa:A5892_18875; -.
DR   KO; K03981; -.
DR   Proteomes; UP000077875; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:UP000077875};
KW   Isomerase {ECO:0000313|EMBL:ANF59786.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077875};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   DOMAIN       19     62       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN       99    223       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   227 AA;  24611 MW;  BC0AEC5D4BC4298E CRC64;
     MAVAADEPPD GLERLTINGT EVAVRDARST PIEGLYRLRL ESGEVVFSDA QGRYMLVGDL
     YENGPGGLVN LSRQAENQER REALASLDED DMVIFRPAGE IKSTLTVFTD TSCPYCHKLH
     AEVPELNQRG IAVRYLAFPR AGENSPGARQ LAQVWCSDNR SEAMSAAVRG EELSASGSAC
     VAQIERDYEL GKRLGVQGTP AVVFPDGSIV PGYLPVDQLT QLIDARS
//
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