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Literature summary for 3.6.4.10 extracted from

  • Krajewska, J.; Arent, Z.; Zolkiewski, M.; K?dzierska-Mieszkowska, S.
    Isolation and identification of putative protein substrates of the AAA+ molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans (2018), Int. J. Mol. Sci., 19, E1234 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Leptospira interrogans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Leptospira interrogans
-
ADP + phosphate
-
?
ATP + H2O Leptospira interrogans B42
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Leptospira interrogans
-
serovar Copenhageni
-
Leptospira interrogans B42
-
serovar Copenhageni
-

Purification (Commentary)

Purification (Comment) Organism
HisPur cobalt resin column chromatography and Superdex S200 gel filtration Leptospira interrogans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Leptospira interrogans ADP + phosphate
-
?
ATP + H2O
-
Leptospira interrogans B42 ADP + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 100000, His6-tagged enzymeSDS-PAGE Leptospira interrogans
? x * 98500, His6-tagged enzyme, calculated from amino acid sequence Leptospira interrogans

Synonyms

Synonyms Comment Organism
ClpB
-
Leptospira interrogans

General Information

General Information Comment Organism
physiological function the enzyme reactivates aggregated proteins in cooperation with the DnaK chaperone system and promotes survival of bacteria under stress conditions. The enzyme can support the virulence of Leptospira interrogans by protecting the conformational integrity and catalytic activity of multiple metabolic enzymes, thus maintaining energy homeostasis in pathogen cells Leptospira interrogans