HSLO_PHOPR
ID HSLO_PHOPR Reviewed; 292 AA.
AC Q6LLS3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=PBPRA3484;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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; CR378674; CAG21755.1; -; Genomic_DNA.
DR RefSeq; WP_011219996.1; NC_006370.1.
DR AlphaFoldDB; Q6LLS3; -.
DR SMR; Q6LLS3; -.
DR STRING; 298386.PBPRA3484; -.
DR EnsemblBacteria; CAG21755; CAG21755; PBPRA3484.
DR KEGG; ppr:PBPRA3484; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_0_0_6; -.
DR OMA; DMQCECC; -.
DR OrthoDB; 1406579at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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; 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..292
FT /note="33 kDa chaperonin"
FT /id="PRO_0000238079"
FT DISULFID 229..231
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 262..265
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 292 AA; 32316 MW; 550486A4247CB71B CRC64;
MTNDNLYRYL FEGVSVRGEL VQLGNTYQQI IASKEYPAPV QKLLGELLVA TSLLTATLKF
EGSITVQLQG DGPVRLAVIN GDHEQKMRGV ARWEGEVPTD GTIHDVIGKG HLVITITPTK
GDRYQGVVGL EGDTLAESLE GYFANSEQLK TRIILRTGEF EGNAKAAGML LQILPDGQGQ
EGDFEHLEQL TETVKDEELF GLDAQDVLYR LYHQEEVKLF DPQSVEFHCG CSRERSASAI
CSIERIEVEK IIADEGKVSL HCDYCGTSYD FDSIDVAALH ENAAKNDRDQ VH