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Database: UniProt
Entry: A0A0B5FTW9_9DELT
LinkDB: A0A0B5FTW9_9DELT
Original site: A0A0B5FTW9_9DELT 
ID   A0A0B5FTW9_9DELT        Unreviewed;       253 AA.
AC   A0A0B5FTW9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   28-FEB-2018, entry version 15.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=GSUB_16600 {ECO:0000313|EMBL:AJF08129.1};
OS   Geoalkalibacter subterraneus.
OG   Plasmid pGSUB1 {ECO:0000313|EMBL:AJF08129.1,
OG   ECO:0000313|Proteomes:UP000035036}.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geoalkalibacter.
OX   NCBI_TaxID=483547 {ECO:0000313|EMBL:AJF08129.1, ECO:0000313|Proteomes:UP000035036};
RN   [1] {ECO:0000313|EMBL:AJF08129.1, ECO:0000313|Proteomes:UP000035036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red1 {ECO:0000313|EMBL:AJF08129.1,
RC   ECO:0000313|Proteomes:UP000035036};
RC   PLASMID=Plasmid pGSUB1 {ECO:0000313|Proteomes:UP000035036};
RX   PubMed=25767222;
RA   Badalamenti J.P., Krajmalnik-Brown R., Torres C.I., Bond D.R.;
RT   "Genomes of Geoalkalibacter ferrihydriticus Z-0531T and
RT   Geoalkalibacter subterraneus Red1T, Two Haloalkaliphilic Metal-
RT   Reducing Deltaproteobacteria.";
RL   Genome Announc. 3:0-0(2015).
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; CP010312; AJF08129.1; -; Genomic_DNA.
DR   RefSeq; WP_040202756.1; NZ_CP010312.1.
DR   EnsemblBacteria; AJF08129; AJF08129; GSUB_16600.
DR   KEGG; gsb:GSUB_16600; -.
DR   KO; K03981; -.
DR   Proteomes; UP000035036; Plasmid pGSUB1.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000035036};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Plasmid {ECO:0000313|EMBL:AJF08129.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035036};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     27       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        28    253       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010002093.
FT   DOMAIN      126    240       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   253 AA;  27895 MW;  0D8BAA48DDCCF2E3 CRC64;
     MTTTYFRKNF IAAAILAFAA ISAPVMAAEQ LPTAMKNLPP GMVDPNKEAV DAMQMIPSEG
     FQMVEANGKT FLLSIDGRYM VRGELHDLWS GQTISSVKQL TDTMDRLDFE KVGLDVQELF
     GLDYGSGDKQ VVVFVAPGCP HCHTLMQKMP ELASEYTFRL IPLPFMGPES VKHTKQVACA
     ADRYPEEATQ ALMSENYDLL PVKEEMCDLD GVRKSLISSK ILGIKGVPYV VSHDKRVSRG
     APRDLKAFLE GGE
//
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