(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILM3_PSEHT

ID   Q3ILM3_PSEHT            Unreviewed;       212 AA.
AC   Q3ILM3;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 87.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   Name=porA {ECO:0000313|EMBL:CAI85352.1};
GN   OrderedLocusNames=PSHAa0249 {ECO:0000313|EMBL:CAI85352.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85352.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85352.1, 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; CAI85352.1; -; Genomic_DNA.
DR   RefSeq; WP_011326966.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILM3; -.
DR   STRING; 326442.PSHAa0249; -.
DR   EnsemblBacteria; CAI85352; CAI85352; PSHAa0249.
DR   GeneID; 32566183; -.
DR   KEGG; pha:PSHAa0249; -.
DR   eggNOG; ENOG4108Z33; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000265316; -.
DR   KO; K03673; -.
DR   OMA; VQSVPAF; -.
DR   OrthoDB; POG091H040A; -.
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; Q3ILM3.
DR   SWISS-2DPAGE; Q3ILM3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW   Isomerase {ECO:0000313|EMBL:CAI85352.1};
KW   Periplasm {ECO:0000256|PIRNR:PIRNR001488};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    212       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004226030.
FT   DOMAIN       12    137       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     52     55       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR001488-1}.
SQ   SEQUENCE   212 AA;  23710 MW;  E4F4E59B8B76E69A CRC64;
     MIKLVKAGLL AVLLPFAATS FAATFEEGVH YEVVSERATK KPEVKEFFSF YCPACNNMEP
     LVAEIKPMLD KGVKFKKSHV DFVGVRDTEH QQMISQALAT AEVLPQKDKI IAAIFSHIHT
     KRANFNELAD VKDVFVAQGV DGDKFDKLFK SFSVRTLSSK MKRDQDYFKE KGALRGVPTF
     IVNGKYKLLL GRESGISEPA DITKLINYLA SK
//

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