ID U4TKN0_9LACO Unreviewed; 291 AA.
AC U4TKN0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=33 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00117};
DE AltName: Full=Heat shock protein 33 homolog {ECO:0000256|HAMAP-Rule:MF_00117};
DE Short=HSP33 {ECO:0000256|HAMAP-Rule:MF_00117};
GN Name=hslO {ECO:0000256|HAMAP-Rule:MF_00117,
GN ECO:0000313|EMBL:ERL63920.1};
GN ORFNames=L248_1811 {ECO:0000313|EMBL:ERL63920.1};
OS Schleiferilactobacillus shenzhenensis LY-73.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL63920.1, ECO:0000313|Proteomes:UP000030647};
RN [1] {ECO:0000313|Proteomes:UP000030647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX PubMed=24265500;
RA Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA Yang R., Liu F.;
RT "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL Genome Announc. 1:e00972-e00913(2013).
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:0000256|HAMAP-Rule:MF_00117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00117}.
CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000256|HAMAP-
CC Rule:MF_00117}.
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DR EMBL; KI271609; ERL63920.1; -; Genomic_DNA.
DR RefSeq; WP_022530817.1; NZ_KI271609.1.
DR AlphaFoldDB; U4TKN0; -.
DR STRING; 1231336.L248_1811; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_1_0_9; -.
DR OrthoDB; 9776534at2; -.
DR Proteomes; UP000030647; Unassembled WGS sequence.
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; 3.55.30.10; Hsp33 domain; 1.
DR Gene3D; 3.90.1280.10; HSP33 redox switch-like; 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 PANTHER; PTHR30111; 33 KDA CHAPERONIN; 1.
DR PANTHER; PTHR30111:SF1; 33 KDA CHAPERONIN; 1.
DR Pfam; PF01430; HSP33; 1.
DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR SUPFAM; SSF64397; Hsp33 domain; 1.
DR SUPFAM; SSF118352; HSP33 redox switch-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00117};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00117};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00117};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00117};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00117}.
FT DISULFID 239..241
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
FT DISULFID 272..275
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00117"
SQ SEQUENCE 291 AA; 30802 MW; 2BE776C57C1168FB CRC64;
MADYLVKAVT TDGHLRALAV DATATVAEAQ RRHDTYGAAS AALGRTLVGT LLLSSALLKD
EGRETLTTRV LGDGPVGAIV AVGKPAGTVK GYIQHPHVQL PLNTVGKIDV RRAVGQGLLA
VSKDMGLKTP FTGQVPLVSG ELAEDFSYYL AQSEQIPSAV GLSVFVQANN TIGAAGGFMI
QALPDAGDAE LAAVEKAVRG LPLISEMMRG GDTPEDILTK IFGESQLKFL DRTPVAFQCD
CSKARFAKSI KALGRHDIEA MINEDHGAEA VCKFCGNKYT YTEDELRNML A
//