ID   HSLO_LACAC              Reviewed;         296 AA.
AC   Q5FMA2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=LBA0279;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42172.1; -; Genomic_DNA.
DR   RefSeq; WP_003549012.1; NC_006814.3.
DR   RefSeq; YP_193203.1; NC_006814.3.
DR   AlphaFoldDB; Q5FMA2; -.
DR   SMR; Q5FMA2; -.
DR   STRING; 272621.LBA0279; -.
DR   PRIDE; Q5FMA2; -.
DR   EnsemblBacteria; AAV42172; AAV42172; LBA0279.
DR   GeneID; 56941882; -.
DR   KEGG; lac:LBA0279; -.
DR   PATRIC; fig|272621.13.peg.264; -.
DR   eggNOG; COG1281; Bacteria.
DR   HOGENOM; CLU_054493_1_0_9; -.
DR   OMA; DMQCECC; -.
DR   BioCyc; LACI272621:G1G49-270-MON; -.
DR   Proteomes; UP000006381; 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; -; 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..296
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000238072"
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   296 AA;  32187 MW;  2915B2DBB3F42C7B CRC64;
     MNDYLVKSID KTKNLRLLTI TAKGVVSEAQ KRHDLWSASS AVLGRTLVGS LLLAGAELTD
     KEELTVRLLG NGPVGPAIVT ATADLKVKGY VKNPHIALPP KENGHIDVKK AVGQGWFEVT
     KDLGLKEPYT GQVPIVSGEI AEDFAYYLTK SEQIPSAVGL SVFVNPNNSI GEAGGFMLQA
     LPGASDALID KTIKRINELP ALSTSFLDGM TPEDLARKIL GTDCKILEKD DVAFSCDCSK
     EKYAGILETL KSSQLKDMIN EDHGAELICN FCGNKYHYTE DELKEILAKK KDDKDY