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Database: UniProt
Entry: F9U624_9GAMM
LinkDB: F9U624_9GAMM
Original site: F9U624_9GAMM 
ID   F9U624_9GAMM            Unreviewed;       255 AA.
AC   F9U624;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-FEB-2018, entry version 25.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=ThimaDRAFT_0375 {ECO:0000313|EMBL:EGV20597.1};
OS   Thiocapsa marina 5811.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Thiocapsa.
OX   NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV20597.1, ECO:0000313|Proteomes:UP000005459};
RN   [1] {ECO:0000313|EMBL:EGV20597.1, ECO:0000313|Proteomes:UP000005459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5811 {ECO:0000313|EMBL:EGV20597.1,
RC   ECO:0000313|Proteomes:UP000005459};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA   Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D., Woyke T.J.;
RT   "The draft genome of Thiocapsa marina 5811.";
RL   Submitted (JUN-2011) 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; AFWV01000001; EGV20597.1; -; Genomic_DNA.
DR   RefSeq; WP_007191253.1; NZ_AFWV01000001.1.
DR   EnsemblBacteria; EGV20597; EGV20597; ThimaDRAFT_0375.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; TMAR768671:G12MV-383-MONOMER; -.
DR   Proteomes; UP000005459; 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   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005459};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   DOMAIN       87    255       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   255 AA;  26714 MW;  3FA646861E265C36 CRC64;
     MRQKLDSPFD ETPGRIARHL GASLAALGLA AASLANPGMA EPLPSTSIAR MAQLPSGGLQ
     AVETTDGELL FFSENGRYVL RGSAVDLWHG AKLTAFDQTQ HLAGRIDLAR LKLDVADLGA
     IDVGEGPEVV VFVDPFCPHC TALYADLAPL RATYRFRLVP IPVLGESSQR AVLALACLSG
     SAPEQARDAL LGGQTADLPE PAAGCGEAVA QRTLIAAQIL GIRGTPFLIA PDGRLHQGRP
     ADLAAWLAAV EERGE
//
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