33 kDa chaperonin

Details

Name
33 kDa chaperonin
Synonyms
  • Heat shock protein 33
  • HSP33
  • yrfI
Gene Name
hslO
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0006216|33 kDa chaperonin
MPQHDQLHRYLFENFAVRGELVTVSETLQQILENHDYPQPVKNVLAELLVATSLLTATLK
FDGDITVQLQGDGPMNLAVINGNNNQQMRGVARVQGEIPENADLKTLVGNGYVVITITPS
EGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGDVDGKPAAGGMLLQVMPAQNA
QQDDFDHLATLTETIKTEELLTLPANEVLWRLYHEEEVTVYDPQDVEFKCTCSRERCADA
LKTLPDEEVDSILAEDGEIDMHCDYCGNHYLFNAMDIAEIRNNASPADPQVH
Number of residues
292
Molecular Weight
32534.245
Theoretical pI
4.1
GO Classification
Functions
identical protein binding
Processes
protein folding / response to heat
Components
cytosol
General Function
Identical protein binding
Specific Function
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0017017|33 kDa chaperonin (hslO)
ATGCCGCAACATGACCAATTACATCGCTATCTGTTTGAAAACTTTGCCGTGCGCGGCGAA
CTGGTAACCGTTTCGGAAACCCTGCAACAGATCCTTGAGAACCACGATTATCCGCAGCCC
GTTAAAAACGTGCTGGCAGAACTGCTGGTTGCGACCAGCCTGTTAACCGCTACGCTGAAG
TTTGATGGTGATATCACCGTACAGCTGCAGGGCGACGGTCCGATGAATCTGGCGGTTATT
AACGGTAACAATAACCAGCAGATGCGCGGTGTGGCGCGCGTGCAGGGCGAAATTCCAGAA
AATGCCGACCTGAAAACGCTGGTCGGCAATGGTTACGTGGTGATCACCATTACCCCGAGC
GAAGGCGAACGCTATCAGGGCGTAGTTGGTCTGGAAGGTGATACCCTGGCGGCCTGCCTG
GAAGATTACTTTATGCGTTCTGAACAGCTGCCGACGCGCCTGTTTATTCGCACCGGCGAC
GTAGACGGCAAACCGGCTGCAGGCGGTATGTTGTTGCAGGTAATGCCTGCGCAAAATGCC
CAGCAGGACGACTTTGACCACCTGGCGACGCTAACCGAAACCATCAAAACCGAAGAACTG
CTGACCTTACCGGCAAACGAAGTGTTGTGGCGTTTGTATCACGAAGAAGAGGTGACGGTT
TACGATCCGCAGGATGTGGAGTTCAAATGCACCTGCTCGCGTGAACGTTGCGCCGATGCG
CTGAAAACGCTGCCTGATGAAGAAGTTGATAGCATCCTGGCGGAAGATGGCGAAATTGAC
ATGCATTGTGATTACTGCGGTAACCACTATCTGTTCAATGCGATGGATATTGCTGAAATC
CGCAACAACGCGTCTCCGGCAGATCCGCAAGTTCATTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A6Y5
UniProtKB Entry NameHSLO_ECOLI
GenBank Gene IDAP009048
General References
  1. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  2. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  3. Jakob U, Muse W, Eser M, Bardwell JC: Chaperone activity with a redox switch. Cell. 1999 Feb 5;96(3):341-52. [Article]
  4. Barbirz S, Jakob U, Glocker MO: Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem. 2000 Jun 23;275(25):18759-66. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails