HSLO_VIBVU
ID HSLO_VIBVU Reviewed; 291 AA.
AC Q8DDS7;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=VV1_0880;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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; AE016795; AAO09383.1; -; Genomic_DNA.
DR RefSeq; WP_011078947.1; NC_004459.3.
DR AlphaFoldDB; Q8DDS7; -.
DR SMR; Q8DDS7; -.
DR EnsemblBacteria; AAO09383; AAO09383; VV1_0880.
DR KEGG; vvu:VV1_0880; -.
DR HOGENOM; CLU_054493_0_0_6; -.
DR OMA; DMQCECC; -.
DR Proteomes; UP000002275; 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; Zinc.
FT CHAIN 1..291
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192224"
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 291 AA; 32632 MW; 1448E5FFE59E85C1 CRC64;
MASNVLNRYL FEDLSVRGEL VQLDEAYQRI ISSKDYPAAL QKLLGELLVS TTLLTATLKF
EGSITIQLQG DGPVSLAVIN GDNEQKIRGV ARWEGHIADD ATLHDMMGKG YMVITIEPKK
GERYQGIVGL EGDNLEQVLE GYFERSEQLK TRIWIRTGEH EGKAHAAGML IQVMPDGTGS
ENDFEHLEQL TNTVKNEELF TLPANELLYR LYNQEQVRLF EPQNVEFRCG CSRERSGAAI
VTVDKNEIYD ILASDGSVSL HCDYCGTTYS FDESDVNKLY EEAASEPKTL H