ID   HSLO_NEIMB              Reviewed;         302 AA.
AC   Q9JXK1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, 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=NMB2000;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF42327.1; -; Genomic_DNA.
DR   PIR; F81016; F81016.
DR   RefSeq; NP_274992.1; NC_003112.2.
DR   RefSeq; WP_010981020.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXK1; -.
DR   SMR; Q9JXK1; -.
DR   STRING; 122586.NMB2000; -.
DR   PaxDb; Q9JXK1; -.
DR   EnsemblBacteria; AAF42327; AAF42327; NMB2000.
DR   KEGG; nme:NMB2000; -.
DR   PATRIC; fig|122586.8.peg.2554; -.
DR   HOGENOM; CLU_054493_0_0_4; -.
DR   OMA; DMQCECC; -.
DR   Proteomes; UP000000425; 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; 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;
KW   Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW   Reference proteome; Zinc.
FT   CHAIN           1..302
FT                   /note="33 kDa chaperonin"
FT                   /id="PRO_0000192187"
FT   DISULFID        234..236
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT   DISULFID        267..270
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ   SEQUENCE   302 AA;  33205 MW;  2C1CF800E1D0DC26 CRC64;
     MNQTAINRAD VRTRFIFDDM PVRGLHVRLE NVWQHIVKQK NYPAAIRRAL GELLAAGVLL
     SGNLKNEGTL IVQVQGRGRL KMLVAEAASD RTVRATARWD ETAEIADDES LGDLLGEGGV
     FVLTLQPKDG EPWQGVVPLE GGGIAQMLVN YMKRSEQLDT HIVLSASDEA AGGLLVQRLP
     EEVLDEEAWE HVSTLARTLT AEELAGLDAQ HVLYRLFHET PPRVFEPETF EFSCTCSRGK
     VSDMLLMLGG EEVGGVVVEQ GSIEVDCDFC HSKYVFDETD VNALFGEDVV GVAKGLPRHT
     VQ