(data stored in SCRATCH zone)

SWISSPROT: Q3KKB0_PSEPF

ID   Q3KKB0_PSEPF            Unreviewed;       213 AA.
AC   Q3KKB0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   OrderedLocusNames=Pfl01_0052 {ECO:0000313|EMBL:ABA71796.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71796.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71796.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71796.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|PIRNR:PIRNR001488}.
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DR   EMBL; CP000094; ABA71796.1; -; Genomic_DNA.
DR   RefSeq; WP_007954043.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0052; -.
DR   EnsemblBacteria; ABA71796; ABA71796; Pfl01_0052.
DR   KEGG; pfo:Pfl01_0052; -.
DR   eggNOG; ENOG4108Z33; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000265318; -.
DR   KO; K03673; -.
DR   OMA; EVVEFFW; -.
DR   BioCyc; PFLU205922:G1G4S-53-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KKB0.
DR   SWISS-2DPAGE; Q3KKB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW   Periplasm {ECO:0000256|PIRNR:PIRNR001488};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    213       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004227508.
FT   DOMAIN        9    152       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     55     58       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR001488-1}.
SQ   SEQUENCE   213 AA;  23089 MW;  4364EADE2D4945CB CRC64;
     MRNLIISAAL VAASLFGVTA QAAEAPAAPY VELSNPVPVA VPGKIEVVEL FWYGCPHCYA
     FEPVINPWVE KLPSDVNFVR IPAMFGGPWD AHGQMFLTLE AMGVEHNVHA AVFNAIQKEH
     KKLTDKNDMA DFLATQGVDK DKFLATFDSF AIKGQIVKAR ELAKKYEISG VPTMIVNGKY
     RFDIGSAGGA EQALKLADQL VAKERATNKA AAN
//

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