HSLO_BACCR
ID HSLO_BACCR Reviewed; 291 AA.
AC Q81J80;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=BC_0074;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP07170.1; -; Genomic_DNA.
DR RefSeq; NP_829969.1; NC_004722.1.
DR RefSeq; WP_000656372.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81J80; -.
DR SMR; Q81J80; -.
DR STRING; 226900.BC_0074; -.
DR EnsemblBacteria; AAP07170; AAP07170; BC_0074.
DR GeneID; 67504759; -.
DR KEGG; bce:BC0074; -.
DR PATRIC; fig|226900.8.peg.89; -.
DR HOGENOM; CLU_054493_1_0_9; -.
DR OMA; DMQCECC; -.
DR Proteomes; UP000001417; 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..291
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192164"
FT DISULFID 237..239
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 270..273
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 291 AA; 32044 MW; 6366BC5617EE5FFB CRC64;
MKDYLVKALA FDGEVRAYSV RTTNTVSEAQ RRHDTWRTAS AALGRSLTAG TMMGAMLKGE
QKLTIKVEGN GPIGPILVDA HANGDVRGYV TNPHVDFEGT EQGKLRVYQA VGTEGFVTVI
KDIGMREPFI GQSPIVSGEL GEDFTYYFAV SEQTPSSVGV GVLVNGDDSI LAAGGFILQI
MPGAQDETIS FIEDRLQKIP PVSTLIEQGL SPEELLYAVL GEDKVKVLET MDVQFNCTCS
RERIESVLIS LGKTELEQVR EEEEETEVHC HFCNERYKFS KEDITNLIEN L