HSLO_THEYD
ID HSLO_THEYD Reviewed; 287 AA.
AC B5YJH3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117};
DE AltName: Full=Heat shock protein 33 homolog {ECO:0000255|HAMAP-Rule:MF_00117};
DE Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117};
GN Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; OrderedLocusNames=THEYE_A0545;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both thermally
CC unfolding and oxidatively damaged proteins from irreversible
CC aggregation. Plays an important role in the bacterial defense system
CC toward oxidative stress. {ECO:0000255|HAMAP-Rule:MF_00117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}.
CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed
CC involving the reactive cysteines. Under reducing conditions zinc is
CC bound to the reactive cysteines and the protein is inactive.
CC {ECO:0000255|HAMAP-Rule:MF_00117}.
CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP-
CC Rule:MF_00117}.
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DR EMBL; CP001147; ACI22197.1; -; Genomic_DNA.
DR RefSeq; WP_012546884.1; NC_011296.1.
DR RefSeq; YP_002248388.1; NC_011296.1.
DR AlphaFoldDB; B5YJH3; -.
DR SMR; B5YJH3; -.
DR STRING; 289376.THEYE_A0545; -.
DR PRIDE; B5YJH3; -.
DR EnsemblBacteria; ACI22197; ACI22197; THEYE_A0545.
DR KEGG; tye:THEYE_A0545; -.
DR PATRIC; fig|289376.4.peg.539; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_0; -.
DR InParanoid; B5YJH3; -.
DR OMA; DMQCECC; -.
DR OrthoDB; 1406579at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd00498; Hsp33; 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 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;
KW Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome; Zinc.
FT CHAIN 1..287
FT /note="33 kDa chaperonin"
FT /id="PRO_1000095040"
FT DISULFID 233..235
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 266..269
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 287 AA; 32215 MW; 8CDF46B8CFB6E5A0 CRC64;
MDEVVKGLIK NEHVLVVATI CTETVEYARK IHDTWPTATA AMGRVIAGSV LLASTLKDRQ
KIMVQIKGDG PLNEVVAEAD SFYRVRAYVK RPHIYMGLKN EKIDVGRGVG KGFLNVIRDL
GLREYYQSSV ELQTGEIARD LAYYLNVSEQ IPSAVSLGVY VEPDNSVKAA GGFMIQTMPE
TRTEIVEFLE RKLSETQSTS SMILQGMDSL QILEEVVGLP IEVLHRGTVT YFCPCTKDRV
INAIVTLGRE EIQKMIEEGK TVDVECYFCK KKYEVTVEEL KILLREI
