Molecular chaperone Hsp31 and glyoxalase 3 (P31658)

Identification
Name:Molecular chaperone Hsp31 and glyoxalase 3
Synonyms:
  • Aminopeptidase HchA
  • D-lactate dehydratase
  • Glyoxalase III
  • Holdase
  • Holding molecular chaperone
Gene Name:hchA
Enzyme Class:
Biological Properties
General Function:Not Available
Specific Function:Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus. Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus.
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Microbial metabolism in diverse environments ec01120
  • Pyruvate metabolism ec00620
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Lactic acid ↔ 1.0Pyruvaldehyde + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Pyruvaldehyde + 1.0Water → 1.0D-Lactic acid + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Lactic acid → 1.0Pyruvaldehyde + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01311D-Lactic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB20598PhenylglyoxalMetaboCard
ECMDB01167PyruvaldehydeMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:Not Available
Gene Properties
Blattner:b1967
Gene OrientationNot Available
Centisome Percentage:Not Available
Left Sequence EndNot Available
Right Sequence EndNot Available
Gene Sequence:
>ENA|AAC75033|AAC75033.1 Escherichia coli str. K-12 substr. MG1655 Glyoxalase III and Hsp31 molecular chaperone
ATGACTGTTCAAACAAGTAAAAATCCGCAGGTCGATATTGCTGAAGATAATGCATTCTTC
CCTTCAGAATATTCGCTTAGCCAATATACCAGTCCTGTCTCTGATCTTGATGGCGTGGAC
TATCCAAAACCTTATCGCGGTAAACATAAAATTCTGGTGATCGCCGCGGACGAACGTTAT
TTGCCGACCGATAACGGAAAACTGTTCTCGACCGGTAACCATCCGATTGAAACGTTGCTG
CCGTTGTATCATCTCCATGCTGCAGGTTTCGAATTCGAAGTGGCGACCATTTCCGGTCTG
ATGACCAAGTTTGAATACTGGGCTATGCCGCACAAAGATGAAAAAGTAATGCCATTCTTT
GAGCAGCATAAATCGTTGTTCCGCAATCCGAAGAAACTCGCGGATGTTGTTGCCAGCCTC
AACGCTGATAGCGAATATGCAGCAATCTTTGTTCCTGGTGGTCATGGCGCACTTATTGGT
TTACCTGAAAGCCAGGACGTGGCTGCCGCTTTACAGTGGGCAATCAAAAATGACCGTTTT
GTTATCTCCCTTTGCCACGGCCCGGCGGCTTTTCTGGCGCTTCGCCACGGCGATAACCCA
CTGAATGGTTATTCCATTTGCGCATTCCCAGACGCCGCAGACAAACAAACGCCAGAGATT
GGCTATATGCCGGGTCATCTCACCTGGTACTTCGGCGAAGAACTGAAGAAAATGGGCATG
AATATCATTAATGACGACATCACCGGGCGAGTACATAAGGACCGTAAACTTCTCACCGGC
GACAGTCCTTTTGCAGCGAATGCGTTGGGTAAACTGGCGGCGCAGGAAATGCTGGCAGCT
TACGCGGGTTAA
Protein Properties
Pfam Domain Function:Not Available
Protein Residues:Not Available
Protein Molecular Weight:Not Available
Protein Theoretical pI:Not Available
Signaling Regions:Not Available
Transmembrane Regions:Not Available
Protein Sequence:
>sp|P31658|HCHA_ECOLI Molecular chaperone Hsp31 and glyoxalase 3 OS=Escherichia coli (strain K12) GN=hchA PE=1 SV=3
MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERY
LPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFF
EQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRF
VISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGM
NIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG
References
External Links:
ResourceLink
Uniprot ID:P31658
ColiBase:b1967
Kegg Gene:b1967
BacMap:16129913
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Kim, O. G., Kim, I. K., Kim, G. H., Ko, J., Park, C., Suh, P. G., Kang, S. O., Lee, H. S., Cha, S. S. (2002). "Crystallization and preliminary X-ray crystallographic analysis of a yedU gene product from Escherichia coli." Acta Crystallogr D Biol Crystallogr 58:1217-1219. Pubmed: 12077448
  • Lee, S. J., Kim, S. J., Kim, I. K., Ko, J., Jeong, C. S., Kim, G. H., Park, C., Kang, S. O., Suh, P. G., Lee, H. S., Cha, S. S. (2003). "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain." J Biol Chem 278:44552-44559. Pubmed: 12939276
  • Malki, A., Caldas, T., Abdallah, J., Kern, R., Eckey, V., Kim, S. J., Cha, S. S., Mori, H., Richarme, G. (2005). "Peptidase activity of the Escherichia coli Hsp31 chaperone." J Biol Chem 280:14420-14426. Pubmed: 15550391
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  • Misra, K., Banerjee, A. B., Ray, S., Ray, M. (1995). "Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione." Biochem J 305 ( Pt 3):999-1003. Pubmed: 7848303
  • Mujacic, M., Bader, M. W., Baneyx, F. (2004). "Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions." Mol Microbiol 51:849-859. Pubmed: 14731284
  • Mujacic, M., Baneyx, F. (2006). "Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31." Mol Microbiol 60:1576-1589. Pubmed: 16796689
  • Mujacic, M., Baneyx, F. (2007). "Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli." Appl Environ Microbiol 73:1014-1018. Pubmed: 17158627
  • Quigley, P. M., Korotkov, K., Baneyx, F., Hol, W. G. (2003). "The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad." Proc Natl Acad Sci U S A 100:3137-3142. Pubmed: 12621151
  • Quigley, P. M., Korotkov, K., Baneyx, F., Hol, W. G. (2004). "A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function." Protein Sci 13:269-277. Pubmed: 14691241
  • Sastry, M. S., Korotkov, K., Brodsky, Y., Baneyx, F. (2002). "Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures." J Biol Chem 277:46026-46034. Pubmed: 12235139
  • Sastry, M. S., Quigley, P. M., Hol, W. G., Baneyx, F. (2004). "The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures." Proc Natl Acad Sci U S A 101:8587-8592. Pubmed: 15173574
  • Subedi, K. P., Choi, D., Kim, I., Min, B., Park, C. (2011). "Hsp31 of Escherichia coli K-12 is glyoxalase III." Mol Microbiol 81:926-936. Pubmed: 21696459
  • Yoshida, T., Ueguchi, C., Yamada, H., Mizuno, T. (1993). "Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant." Mol Gen Genet 237:113-122. Pubmed: 8455549
  • Zhao, Y., Liu, D., Kaluarachchi, W. D., Bellamy, H. D., White, M. A., Fox, R. O. (2003). "The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites." Protein Sci 12:2303-2311. Pubmed: 14500888