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Database: UniProt
Entry: E8RVX5_ASTEC
LinkDB: E8RVX5_ASTEC
Original site: E8RVX5_ASTEC 
ID   E8RVX5_ASTEC            Unreviewed;       268 AA.
AC   E8RVX5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   25-APR-2018, entry version 36.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   OrderedLocusNames=Astex_3787 {ECO:0000313|EMBL:ADU15397.1};
OS   Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / VKM B-1370 /
OS   CB 48).
OG   Plasmid pASTEX02 {ECO:0000313|EMBL:ADU15397.1,
OG   ECO:0000313|Proteomes:UP000001492}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU15397.1, ECO:0000313|Proteomes:UP000001492};
RN   [1] {ECO:0000313|Proteomes:UP000001492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48
RC   {ECO:0000313|Proteomes:UP000001492};
RC   PLASMID=Plasmid pASTEX02 {ECO:0000313|Proteomes:UP000001492};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brun Y.V., Woyke T.;
RT   "Complete sequence of plasmid 2 of Asticcacaulis excentricus CB 48.";
RL   Submitted (DEC-2010) 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; CP002398; ADU15397.1; -; Genomic_DNA.
DR   RefSeq; WP_013481210.1; NC_014819.1.
DR   ProteinModelPortal; E8RVX5; -.
DR   EnsemblBacteria; ADU15397; ADU15397; Astex_3787.
DR   KEGG; aex:Astex_3787; -.
DR   KO; K03981; -.
DR   OMA; EINRIKW; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; AEXC573065:G1GPE-3791-MONOMER; -.
DR   Proteomes; UP000001492; Plasmid pASTEX02.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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/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:UP000001492};
KW   Isomerase {ECO:0000313|EMBL:ADU15397.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Plasmid {ECO:0000313|EMBL:ADU15397.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001492};
KW   Signal {ECO:0000256|RuleBase:RU364038};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      9     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       37     90       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      146    259       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   268 AA;  28038 MW;  BD59678C6BE57800 CRC64;
     MLPLSKPKLI VPAMLALVAI AVTGTFLLGP KTEETVKTKI AAHFPNSTVN SVSCKTAIGL
     CEVVMGKNLL YATRDGRYVV VGAVLDLKAR KDLTDQRLKE LAAVDAATTS VEGQRVEAPV
     KAAAGKLSVT LPKANAVIHN PGAPLKMTVF GDYSCGYCHQ LFAQLAGTTN IEITEYPIAI
     LGPQSAEKAR LVMCAGDRAA AAEAAYTGGE IKTGADCAKF DAVIAENTRF AQANGINGTP
     AIIRADGTVN AGFLPLPDLI RFLEGKNV
//
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