SWISSPROT: Q4ZZT1_PSEU2

ID   Q4ZZT1_PSEU2            Unreviewed;       214 AA.
AC   Q4ZZT1;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   OrderedLocusNames=Psyr_0268 {ECO:0000313|EMBL:AAY35341.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35341.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35341.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35341.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35341.1; -; Genomic_DNA.
DR   RefSeq; WP_003403888.1; NC_007005.1.
DR   RefSeq; YP_233379.1; NC_007005.1.
DR   STRING; 205918.Psyr_0268; -.
DR   EnsemblBacteria; AAY35341; AAY35341; Psyr_0268.
DR   GeneID; 3365744; -.
DR   KEGG; psb:Psyr_0268; -.
DR   PATRIC; fig|205918.7.peg.268; -.
DR   eggNOG; ENOG4108Z33; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000265318; -.
DR   KO; K03673; -.
DR   OMA; EVVEFFW; -.
DR   BioCyc; PSYR205918:G1G4J-269-MONOMER; -.
DR   Proteomes; UP000000426; 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; Q4ZZT1.
DR   SWISS-2DPAGE; Q4ZZT1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
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    214       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004247822.
FT   DOMAIN       12    154       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     57     60       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR001488-1}.
SQ   SEQUENCE   214 AA;  23210 MW;  CFBC15423BBFCD15 CRC64;
     MRNLIISAAL VAASLFGMSA QAATPIEAGK QYVELASAVP VAEPGKIEVV ELFWYGCPHC
     YAFEPTINPW VEKLPSDVKF VRIPAMFGGP WDAHGQLFIT LDTMGVEHKV HAAVFEAIQK
     GGKRLTDKND MADFVATQGV NKEDFLKTFD SFAVKGKIAQ YKELAKKYEV TGVPTMIVNG
     KYRFDLGSAG GPEKTLEVAD QLIAKERAAA AAAK
//