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Database: UniProt
Entry: B2UDL5_RALPJ
LinkDB: B2UDL5_RALPJ
Original site: B2UDL5_RALPJ 
ID   B2UDL5_RALPJ            Unreviewed;       248 AA.
AC   B2UDL5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   18-JUL-2018, entry version 57.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   OrderedLocusNames=Rpic_3134 {ECO:0000313|EMBL:ACD28256.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD28256.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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; CP001068; ACD28256.1; -; Genomic_DNA.
DR   RefSeq; WP_009241994.1; NC_010682.1.
DR   ProteinModelPortal; B2UDL5; -.
DR   STRING; 402626.Rpic_3134; -.
DR   EnsemblBacteria; ACD28256; ACD28256; Rpic_3134.
DR   GeneID; 6286164; -.
DR   KEGG; rpi:Rpic_3134; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   HOGENOM; HOG000222078; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   BioCyc; RPIC402626:GH94-3137-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 1.
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; 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:UP000002566};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     29       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        30    248       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010007641.
FT   DOMAIN       39     91       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      120    240       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   248 AA;  26581 MW;  DA2BAB1BE8446EE1 CRC64;
     MSFRIRVAAI ASAVAVAAIG AGYVLSAGAA EPALDKVKAT VQKALGPNVE IKSVTKSPLA
     GLYEINLGSQ VVYSDATGRY VLNGDLLDTQ TATNLTQERL AELNRVKWSD LPLDRAVKWV
     KGNGARKIAV FSDPNCPYCH KLEQMLTQVD NVTVYTFLFP ILSEDSNTKA KQIWCSADRA
     KAWRDWMTAK TAPGGAGTCD TPLEANLKLG QQLNVTGTPA IIFPDGSRAP GLIDAATLER
     KFAALKKS
//
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