(data stored in SCRATCH zone)

SWISSPROT: A0KFS3_AERHH

ID   A0KFS3_AERHH            Unreviewed;       295 AA.
AC   A0KFS3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=33 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00117};
DE   AltName: Full=Heat shock protein 33 homolog {ECO:0000256|HAMAP-Rule:MF_00117};
DE            Short=HSP33 {ECO:0000256|HAMAP-Rule:MF_00117};
GN   Name=hslO {ECO:0000256|HAMAP-Rule:MF_00117,
GN   ECO:0000313|EMBL:ABK39863.1};
GN   OrderedLocusNames=AHA_0566 {ECO:0000313|EMBL:ABK39863.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39863.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39863.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Redox regulated molecular chaperone. Protects both
CC       thermally unfolding and oxidatively damaged proteins from
CC       irreversible aggregation. Plays an important role in the bacterial
CC       defense system toward oxidative stress. {ECO:0000256|HAMAP-
CC       Rule:MF_00117, ECO:0000256|SAAS:SAAS01084509}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117,
CC       ECO:0000256|SAAS:SAAS01084524}.
CC   -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC       involving the reactive cysteines. Under reducing conditions zinc
CC       is bound to the reactive cysteines and the protein is inactive.
CC       {ECO:0000256|HAMAP-Rule:MF_00117}.
CC   -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00117, ECO:0000256|SAAS:SAAS01084516}.
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DR   EMBL; CP000462; ABK39863.1; -; Genomic_DNA.
DR   RefSeq; WP_011704537.1; NC_008570.1.
DR   RefSeq; YP_855099.1; NC_008570.1.
DR   STRING; 380703.AHA_0566; -.
DR   EnsemblBacteria; ABK39863; ABK39863; AHA_0566.
DR   GeneID; 4489388; -.
DR   KEGG; aha:AHA_0566; -.
DR   PATRIC; fig|380703.7.peg.560; -.
DR   eggNOG; ENOG4105F4C; Bacteria.
DR   eggNOG; COG1281; LUCA.
DR   HOGENOM; HOG000261998; -.
DR   KO; K04083; -.
DR   OMA; DMQCECC; -.
DR   BioCyc; AHYD380703:G1G7B-567-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00498; Hsp33; 1.
DR   Gene3D; 1.10.287.480; -; 1.
DR   Gene3D; 3.55.30.10; -; 1.
DR   Gene3D; 3.90.1280.10; -; 1.
DR   HAMAP; MF_00117; HslO; 1.
DR   InterPro; IPR000397; Heat_shock_Hsp33.
DR   InterPro; IPR016154; Heat_shock_Hsp33_C.
DR   InterPro; IPR016153; Heat_shock_Hsp33_N.
DR   InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom_sf.
DR   PANTHER; PTHR30111; PTHR30111; 1.
DR   Pfam; PF01430; HSP33; 1.
DR   PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR   SUPFAM; SSF118352; SSF118352; 1.
DR   SUPFAM; SSF64397; SSF64397; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFS3.
DR   SWISS-2DPAGE; A0KFS3.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084514};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084515};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084518};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00117,
KW   ECO:0000256|SAAS:SAAS01084519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00117, ECO:0000256|SAAS:SAAS01084517}.
FT   DISULFID    232    234       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00117}.
FT   DISULFID    265    268       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00117}.
SQ   SEQUENCE   295 AA;  33443 MW;  B0519DAEA98B7460 CRC64;
     MMSNQDLLYR YLFEEYEVRG ELVQLDHTYR HVVEAQNYPV QVQKLLGELL VATSLLTATL
     KFEGSITVQL QGNGPVRLAV INGDNNQQLR GVARYEGELP SDDKLQSLIG EGQLVITITP
     EQGERYQGII ALDADTLAGC LEHYFAQSEQ LATKLWIRTG YHQGEPRAAG ILLQELPAQS
     EDHSDDFEHL TQLTSTIKDE ELFGLEAEEI LYRLYHQDKV RVFDPQAVEF RCTCSRARCE
     GALLQIEKEE VMEMVQELGK IDMHCDYCGA QYQFDGIDVE TLFSRAPGND ANKLH
//

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