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Database: UniProt
Entry: A0A066RJF1_9GAMM
LinkDB: A0A066RJF1_9GAMM
Original site: A0A066RJF1_9GAMM 
ID   A0A066RJF1_9GAMM        Unreviewed;       240 AA.
AC   A0A066RJF1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   22-NOV-2017, entry version 20.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=EA58_17210 {ECO:0000313|EMBL:KDM90464.1};
OS   Photobacterium galatheae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=1654360 {ECO:0000313|EMBL:KDM90464.1, ECO:0000313|Proteomes:UP000027192};
RN   [1] {ECO:0000313|EMBL:KDM90464.1, ECO:0000313|Proteomes:UP000027192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2753 {ECO:0000313|EMBL:KDM90464.1,
RC   ECO:0000313|Proteomes:UP000027192};
RA   Machado H.R., Gram L.;
RT   "Draft genome sequence of Photobacterium halotolerans S2753: a
RT   solonamide, ngercheumicin and holomycin producer.";
RL   Submitted (APR-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:KDM90464.1}.
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DR   EMBL; JMIB01000032; KDM90464.1; -; Genomic_DNA.
DR   RefSeq; WP_036755223.1; NZ_JMIB01000032.1.
DR   ProteinModelPortal; A0A066RJF1; -.
DR   EnsemblBacteria; KDM90464; KDM90464; EA58_17210.
DR   Proteomes; UP000027192; Unassembled WGS sequence.
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   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_N.
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:UP000027192};
KW   Isomerase {ECO:0000313|EMBL:KDM90464.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027192};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     22       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        23    240       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010008593.
FT   DOMAIN       35     77       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      111    236       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   240 AA;  26224 MW;  F798646A945DE767 CRC64;
     MPFSCRPLLV ALAAFTAFSA SAEPNARAIE ATLSPLGLTA ASVKPSPIQG MSEVVTERGI
     IYMSDDGQYF LAGHLYQSVN GEPVNLTEQK LASINKDKLK NMTGEMIVYP AKDEKYVVTV
     FTDTSCGYCR KLHSEMQAYN DAGITIRYLA FPRGGERSQN FDEMSAIWAA KDRVKAMDEA
     KKGKLDIEQS PHNDALVMKH YQLGVAMGVS GTPALVLEDG TMLPGYQPAS RLLQFLNSRS
//
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