HSLO_YERPN
ID HSLO_YERPN Reviewed; 293 AA.
AC Q1CCM7; D1Q2U3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=YPN_3926;
GN ORFNames=YP516_4456;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG20253.1; -; Genomic_DNA.
DR EMBL; ACNQ01000019; EEO74846.1; -; Genomic_DNA.
DR RefSeq; WP_002208911.1; NZ_ACNQ01000019.1.
DR AlphaFoldDB; Q1CCM7; -.
DR SMR; Q1CCM7; -.
DR EnsemblBacteria; ABG20253; ABG20253; YPN_3926.
DR GeneID; 66843815; -.
DR KEGG; ypn:YPN_3926; -.
DR HOGENOM; CLU_054493_0_0_6; -.
DR OMA; DMQCECC; -.
DR Proteomes; UP000008936; 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; 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; Zinc.
FT CHAIN 1..293
FT /note="33 kDa chaperonin"
FT /id="PRO_1000015595"
FT DISULFID 231..233
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
FT DISULFID 264..267
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117"
SQ SEQUENCE 293 AA; 32478 MW; 8074381C35AD99AC CRC64;
MSNHDQLHRY LFANHAVRGE LVSVNETYQQ VLANHDYPPA VQKLLGEMLV ATSLLTATLK
FDGDITVQLQ GGDGPLTLAV INGNNRQEMR GVARVKGEIS DDSTLQEMVG NGYLVITITP
AQGERYQGVV ALEGETIAAC LENYFMQSEQ LPTRLFIRTG HVADKAAAGG MLLQVLPAQE
RNEDEFDHLA QLTATIKAEE LFTLPANEVL YRLYHQEEVT LYEPQNVSFR CTCSRQRCAD
ALVTLADDDV TEMLEQDGNI DMHCEYCGNH YLFDAVDIAT LKNGNSASSE QIH