HSLO_ECOLI
ID HSLO_ECOLI Reviewed; 292 AA.
AC P0A6Y5; P45803; Q2M766;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117};
DE AltName: Full=Heat shock protein 33;
DE Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117};
GN Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; Synonyms=yrfI;
GN OrderedLocusNames=b3401, JW5692;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10025400; DOI=10.1016/s0092-8674(00)80547-4;
RA Jakob U., Muse W., Eser M., Bardwell J.C.A.;
RT "Chaperone activity with a redox switch.";
RL Cell 96:341-352(1999).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=10764757; DOI=10.1074/jbc.m001089200;
RA Barbirz S., Jakob U., Glocker M.O.;
RT "Mass spectrometry unravels disulfide bond formation as the mechanism that
RT activates a molecular chaperone.";
RL J. Biol. Chem. 275:18759-18766(2000).
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.
CC -!- INTERACTION:
CC P0A6Y5; P0A6Y5: hslO; NbExp=5; IntAct=EBI-562857, EBI-562857;
CC P0A6Y5; P0CE47: tufA; NbExp=3; IntAct=EBI-562857, EBI-301077;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock.
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 -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP-
CC Rule:MF_00117}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58198.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA58198.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76426.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77890.1; -; Genomic_DNA.
DR PIR; D65135; D65135.
DR RefSeq; NP_417860.2; NC_000913.3.
DR RefSeq; WP_001135574.1; NZ_STEB01000004.1.
DR PDB; 1HW7; X-ray; 2.20 A; A=1-253.
DR PDB; 1I7F; X-ray; 2.70 A; A=1-292.
DR PDB; 1XJH; NMR; -; A=225-285.
DR PDB; 3M7M; X-ray; 2.90 A; X=1-233.
DR PDBsum; 1HW7; -.
DR PDBsum; 1I7F; -.
DR PDBsum; 1XJH; -.
DR PDBsum; 3M7M; -.
DR AlphaFoldDB; P0A6Y5; -.
DR SMR; P0A6Y5; -.
DR BioGRID; 4262486; 11.
DR DIP; DIP-48013N; -.
DR IntAct; P0A6Y5; 11.
DR MINT; P0A6Y5; -.
DR STRING; 511145.b3401; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR jPOST; P0A6Y5; -.
DR PaxDb; P0A6Y5; -.
DR PRIDE; P0A6Y5; -.
DR EnsemblBacteria; AAC76426; AAC76426; b3401.
DR EnsemblBacteria; BAE77890; BAE77890; BAE77890.
DR GeneID; 67417028; -.
DR GeneID; 947178; -.
DR KEGG; ecj:JW5692; -.
DR KEGG; eco:b3401; -.
DR PATRIC; fig|1411691.4.peg.3329; -.
DR EchoBASE; EB2766; -.
DR eggNOG; COG1281; Bacteria.
DR HOGENOM; CLU_054493_0_0_6; -.
DR InParanoid; P0A6Y5; -.
DR OMA; DMQCECC; -.
DR PhylomeDB; P0A6Y5; -.
DR BioCyc; EcoCyc:G7744-MON; -.
DR EvolutionaryTrace; P0A6Y5; -.
DR PRO; PR:P0A6Y5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044183; F:protein folding chaperone; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0036506; P:maintenance of unfolded protein; IDA:EcoCyc.
DR GO; GO:0042026; P:protein refolding; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR GO; GO:0006979; P:response to oxidative stress; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome; Stress response; Zinc.
FT CHAIN 1..292
FT /note="33 kDa chaperonin"
FT /id="PRO_0000192174"
FT DISULFID 230..232
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117,
FT ECO:0000269|PubMed:10764757"
FT DISULFID 263..266
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00117,
FT ECO:0000269|PubMed:10764757"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1HW7"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1HW7"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1HW7"
FT HELIX 39..56
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 60..75
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1HW7"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 110..122
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1HW7"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:1HW7"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3M7M"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:1HW7"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:1HW7"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1HW7"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3M7M"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:1XJH"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:1XJH"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:1XJH"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1XJH"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:1XJH"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:1XJH"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1XJH"
SQ SEQUENCE 292 AA; 32534 MW; 18F05BD2F0257552 CRC64;
MPQHDQLHRY LFENFAVRGE LVTVSETLQQ ILENHDYPQP VKNVLAELLV ATSLLTATLK
FDGDITVQLQ GDGPMNLAVI NGNNNQQMRG VARVQGEIPE NADLKTLVGN GYVVITITPS
EGERYQGVVG LEGDTLAACL EDYFMRSEQL PTRLFIRTGD VDGKPAAGGM LLQVMPAQNA
QQDDFDHLAT LTETIKTEEL LTLPANEVLW RLYHEEEVTV YDPQDVEFKC TCSRERCADA
LKTLPDEEVD SILAEDGEID MHCDYCGNHY LFNAMDIAEI RNNASPADPQ VH
