HSLO_HAEIN
ID HSLO_HAEIN Reviewed; 293 AA.
AC P44877;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=HI_0810;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22469.1; -; Genomic_DNA.
DR PIR; H64158; H64158.
DR RefSeq; NP_438970.1; NC_000907.1.
DR RefSeq; WP_005693176.1; NC_000907.1.
DR AlphaFoldDB; P44877; -.
DR SMR; P44877; -.
DR STRING; 71421.HI_0810; -.
DR EnsemblBacteria; AAC22469; AAC22469; HI_0810.
DR KEGG; hin:HI_0810; -.
DR PATRIC; fig|71421.8.peg.851; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_0_0_6; -.
DR OMA; DMQCECC; -.
DR PhylomeDB; P44877; -.
DR BioCyc; HINF71421:G1GJ1-851-MON; -.
DR Proteomes; UP000000579; 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..293
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192180"
FT DISULFID 237..239
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 271..274
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 293 AA; 33103 MW; 05C25281B6CCE96A CRC64;
MTNQQDYTQD NDKLYRYLFQ HRAVRGEWVR LNKTFTDTLN THQYPKAVQD LLGEMMVATN
LLTATLKFAG NITVQIQGDG PLRLALVNGN DQQQIRALAR VDGNITENMS LHNMIGKGVL
VITIAPKEGE RYQGVISLDK PTITECLEDY FVRSEQLQTQ LIIRTGEYEG KPVAAGMLLQ
IMPDGSGTPE DFEHLTTLAA TVKDEELFGL PAEELLYRLY HEETVNLYPA QDVQFFCGCS
AERSSSALLL ISDEEIDEIL AEHKGRIDMQ CECCGTHYFF NKEAIEKLKS TRV