ID HSLO_LACLA Reviewed; 288 AA.
AC Q9CE86;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=LL1959;
GN ORFNames=L17654;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK06057.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005176; AAK06057.1; ALT_INIT; Genomic_DNA.
DR PIR; G86869; G86869.
DR RefSeq; NP_268116.2; NC_002662.1.
DR RefSeq; WP_010906231.1; NC_002662.1.
DR AlphaFoldDB; Q9CE86; -.
DR SMR; Q9CE86; -.
DR PaxDb; 272623-L17654; -.
DR EnsemblBacteria; AAK06057; AAK06057; L17654.
DR KEGG; lla:L17654; -.
DR PATRIC; fig|272623.7.peg.2109; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_9; -.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000002196; 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; 3.55.30.10; Hsp33 domain; 1.
DR Gene3D; 3.90.1280.10; HSP33 redox switch-like; 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; 33 KDA CHAPERONIN; 1.
DR PANTHER; PTHR30111:SF1; 33 KDA CHAPERONIN; 1.
DR Pfam; PF01430; HSP33; 1.
DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR SUPFAM; SSF64397; Hsp33 domain; 1.
DR SUPFAM; SSF118352; HSP33 redox switch-like; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome; Zinc.
FT CHAIN 1..288
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192181"
FT DISULFID 236..238
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 269..272
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 288 AA; 31719 MW; E6A6859608CA85BE CRC64;
MDKIIKSISK NGHFRAFALD STLTVKEAQE RHQTWPTSTV ALGRTLIAGQ ILGANEKGDT
KITVKVLGDG AMGPIIAVAD SRGHVKGYVK NRKLDYKKAS TGEVLVAPFV GNGFLVVVKD
MGLKQPYSGQ VDLITGEIGE DLAWYFLSSE QTPSSVGVNV LLNEDSDTVK IAGGFMLQAL
PDATDEEITE IEHNIKSMPS IATMLTSEEP LKTMLDNIYG DMEYKNLGEF PLEFKCDCSK
ERFLEGIKSL GREPIEEMIA EDHGAEIICQ FCENKYEYSE DELKALLK
//
