(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILM4_PSEHT

ID   Q3ILM4_PSEHT            Unreviewed;       207 AA.
AC   Q3ILM4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 89.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   Name=dsbA {ECO:0000313|EMBL:CAI85351.1};
GN   OrderedLocusNames=PSHAa0248 {ECO:0000313|EMBL:CAI85351.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85351.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85351.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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; CR954246; CAI85351.1; -; Genomic_DNA.
DR   RefSeq; WP_011326965.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILM4; -.
DR   SMR; Q3ILM4; -.
DR   STRING; 326442.PSHAa0248; -.
DR   EnsemblBacteria; CAI85351; CAI85351; PSHAa0248.
DR   KEGG; pha:PSHAa0248; -.
DR   PATRIC; fig|326442.8.peg.239; -.
DR   eggNOG; ENOG4108Z33; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000265316; -.
DR   KO; K03673; -.
DR   OMA; EVVEFFW; -.
DR   OrthoDB; POG091H03L9; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILM4.
DR   SWISS-2DPAGE; Q3ILM4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW   Isomerase {ECO:0000313|EMBL:CAI85351.1};
KW   Periplasm {ECO:0000256|PIRNR:PIRNR001488};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    207       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004225889.
FT   DOMAIN        7    206       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     50     53       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR001488-1}.
SQ   SEQUENCE   207 AA;  22992 MW;  76A82D7E286C4D9C CRC64;
     MLKKLKLSLL LLCLPFAALA ANFEVGNQYT VIDIEKSTTP QVTEYFSFYC PHCFKFEPVA
     HAIEENLPAG AVFIKNHVNF LGGVSPQTQS NLSLAYLVAK KHGQADTITD KIFKSIHVQR
     APLTEIKDLK KLLDINGISS DTFDQDIASM PIIAAEQAMQ DKQNKYSKLG ALTGVPTFIV
     NDKYKINLNT IKSQEELDEL VSFLLAL
//

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