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Database: UniProt
Entry: C7RQD1_ACCPU
LinkDB: C7RQD1_ACCPU
Original site: C7RQD1_ACCPU 
ID   C7RQD1_ACCPU            Unreviewed;       237 AA.
AC   C7RQD1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   25-APR-2018, entry version 50.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   OrderedLocusNames=CAP2UW1_4302 {ECO:0000313|EMBL:ACV37538.1};
OS   Accumulibacter phosphatis (strain UW-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria;
OC   Candidatus Accumulibacter.
OX   NCBI_TaxID=522306 {ECO:0000313|EMBL:ACV37538.1, ECO:0000313|Proteomes:UP000001619};
RN   [1] {ECO:0000313|EMBL:ACV37538.1, ECO:0000313|Proteomes:UP000001619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UW-1 {ECO:0000313|EMBL:ACV37538.1,
RC   ECO:0000313|Proteomes:UP000001619};
RG   US DOE Joint Genome Institute;
RA   Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S.,
RA   Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S.,
RA   Kyrpides N.C., McMahon K.D., Hugenholtz P.;
RT   "Complete sequence of chromosome of Candidatus Accumulibacter
RT   phosphatis clade IIA str. UW-1.";
RL   Submitted (SEP-2009) 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; CP001715; ACV37538.1; -; Genomic_DNA.
DR   RefSeq; WP_015768693.1; NC_013194.1.
DR   ProteinModelPortal; C7RQD1; -.
DR   STRING; 522306.CAP2UW1_4302; -.
DR   EnsemblBacteria; ACV37538; ACV37538; CAP2UW1_4302.
DR   KEGG; app:CAP2UW1_4302; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   HOGENOM; HOG000222078; -.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; CACC522306:G12V9-4222-MONOMER; -.
DR   Proteomes; UP000001619; Chromosome.
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   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   InterPro; IPR017937; Thioredoxin_CS.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001619};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001619};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     20       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        21    237       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010000550.
FT   DOMAIN       26     77       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      107    229       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   237 AA;  25809 MW;  9155739BCB1303FF CRC64;
     MYKKLIPFAL AAFLSLPTLA DEASVKKAVE AKIGGPVTSV TKTTYLGLYE VYADGQVLYT
     DEKVSALLIG SLIDGKTMRN VTTERMQKLT AIKFSELPLA NAIKQVRGDG KRVFASFEDP
     NCGYCKKMAK EIAKLDNVTV YTFLYPILSP DSLEKSNQIW CASDRVKAWN DWMVDGKAPA
     GKGDCDTTAI KTTLETGRKL AINGTPTIFF ADGERVPGAI PLARIEQKLA QTPSSGK
//
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