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Literature summary extracted from

  • Kedzierska-Mieszkowska, S.; Zolkiewski, M.
    Hsp100 molecular chaperone ClpB and its role invirulence of bacterial pathogens (2021), Int. J. Mol. Sci., 22, 5319.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Enterococcus faecalis
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Francisella tularensis
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Leptospira interrogans
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Listeria monocytogenes
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Mycobacterium tuberculosis
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Mycoplasmoides pneumoniae
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Porphyromonas gingivalis
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Staphylococcus aureus
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Escherichia coli
3.6.4.10 drug development ClpB is not found in human cells, and is thus an attractive target for antimicrobial therapies in combating bacterial infections Ehrlichia chaffeensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.10 Mg2+ required Ehrlichia chaffeensis
3.6.4.10 Mg2+ required Enterococcus faecalis
3.6.4.10 Mg2+ required Escherichia coli
3.6.4.10 Mg2+ required Francisella tularensis
3.6.4.10 Mg2+ required Leptospira interrogans
3.6.4.10 Mg2+ required Listeria monocytogenes
3.6.4.10 Mg2+ required Mycobacterium tuberculosis
3.6.4.10 Mg2+ required Mycoplasmoides pneumoniae
3.6.4.10 Mg2+ required Porphyromonas gingivalis
3.6.4.10 Mg2+ required Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 Mg2+ required Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.10 ATP + H2O Enterococcus faecalis
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Francisella tularensis
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Leptospira interrogans
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Listeria monocytogenes
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Mycobacterium tuberculosis
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Mycoplasmoides pneumoniae
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Porphyromonas gingivalis
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Staphylococcus aureus
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Escherichia coli
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Ehrlichia chaffeensis
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Mycobacterium tuberculosis H37Rv
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Enterococcus faecalis ATCC 700802
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Mycobacterium tuberculosis ATCC 25618
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Escherichia coli K12
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Ehrlichia chaffeensis ATCC CRL-10679
-
 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O Ehrlichia chaffeensis Arkansas
-
 ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.10 Ehrlichia chaffeensis Q2GH96
-
-
3.6.4.10 Ehrlichia chaffeensis Arkansas Q2GH96
-
-
3.6.4.10 Ehrlichia chaffeensis ATCC CRL-10679 Q2GH96
-
-
3.6.4.10 Enterococcus faecalis Q831Y7
-
-
3.6.4.10 Enterococcus faecalis ATCC 700802 Q831Y7
-
-
3.6.4.10 Escherichia coli P63284
-
-
3.6.4.10 Escherichia coli K12 P63284
-
-
3.6.4.10 Francisella tularensis A0A6I4RTM2
-
-
3.6.4.10 Leptospira interrogans
-
-
-
3.6.4.10 Listeria monocytogenes
-
-
-
3.6.4.10 Mycobacterium tuberculosis P9WPD1
-
-
3.6.4.10 Mycobacterium tuberculosis ATCC 25618 P9WPD1
-
-
3.6.4.10 Mycobacterium tuberculosis H37Rv P9WPD1
-
-
3.6.4.10 Mycoplasmoides pneumoniae A0AAV5N8R9 Mycoplasma pneumoniae
-
3.6.4.10 no ClpB activity in Homo sapiens
-
-
-
3.6.4.10 Porphyromonas gingivalis
-
 Bacteroides gingivalis
-
3.6.4.10 Salmonella enterica subsp. enterica serovar Typhimurium Q7CQ01
-
-
3.6.4.10 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 Q7CQ01
-
-
3.6.4.10 Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 Q7CQ01
-
-
3.6.4.10 Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.10 ATP + H2O
-
 Enterococcus faecalis ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Francisella tularensis ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Leptospira interrogans ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Listeria monocytogenes ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Mycobacterium tuberculosis ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Mycoplasmoides pneumoniae ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Porphyromonas gingivalis ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Staphylococcus aureus ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Escherichia coli ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Ehrlichia chaffeensis ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Enterococcus faecalis ATCC 700802 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Mycobacterium tuberculosis ATCC 25618 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Escherichia coli K12 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Ehrlichia chaffeensis ATCC CRL-10679 ADP + phosphate
-
 ?
3.6.4.10 ATP + H2O
-
 Ehrlichia chaffeensis Arkansas ADP + phosphate
-
 ?
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Enterococcus faecalis ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Francisella tularensis ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Leptospira interrogans ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Listeria monocytogenes ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Mycobacterium tuberculosis ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Mycoplasmoides pneumoniae ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Porphyromonas gingivalis ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Staphylococcus aureus ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Salmonella enterica subsp. enterica serovar Typhimurium ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Escherichia coli ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Ehrlichia chaffeensis ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Mycobacterium tuberculosis H37Rv ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Enterococcus faecalis ATCC 700802 ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Mycobacterium tuberculosis ATCC 25618 ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Escherichia coli K12 ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Ehrlichia chaffeensis ATCC CRL-10679 ?
-
-
3.6.4.10 additional information structure and reaction mechanism of ClpB, overview Ehrlichia chaffeensis Arkansas ?
-
-

Subunits

EC Number Subunits Comment Organism
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Enterococcus faecalis
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Francisella tularensis
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Leptospira interrogans
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Listeria monocytogenes
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Mycobacterium tuberculosis
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Mycoplasmoides pneumoniae
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Porphyromonas gingivalis
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Staphylococcus aureus
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Escherichia coli
3.6.4.10 hexamer ClpB forms ring-shaped hexamers in the presence of ATP with a narrow central channel (pore), wide enough to accommodate extended unfolded polypeptides, structural organization of the ClpB monomer, overview. Four domains are indicated: N-terminal domain (NTD), two nucleotide-binding domains (NBD-1 and NBD-2), and middle domain (MD). Each NBD contains the characteristic AAA+ motifs: Walker A (GX4GKT/S), Walker B (Hy2DE), sensor-1 (S-1), sensor-2 (S-2, GAR), and the arginine fingers Ehrlichia chaffeensis

Synonyms

EC Number Synonyms Comment Organism
3.6.4.10 AAA+ ATPase
-
 Enterococcus faecalis
3.6.4.10 AAA+ ATPase
-
 Francisella tularensis
3.6.4.10 AAA+ ATPase
-
 Leptospira interrogans
3.6.4.10 AAA+ ATPase
-
 Listeria monocytogenes
3.6.4.10 AAA+ ATPase
-
 Mycobacterium tuberculosis
3.6.4.10 AAA+ ATPase
-
 Mycoplasmoides pneumoniae
3.6.4.10 AAA+ ATPase
-
 Porphyromonas gingivalis
3.6.4.10 AAA+ ATPase
-
 Staphylococcus aureus
3.6.4.10 AAA+ ATPase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 AAA+ ATPase
-
 Escherichia coli
3.6.4.10 AAA+ ATPase
-
 Ehrlichia chaffeensis
3.6.4.10 ATP-dependent chaperone ClpB UniProt Mycoplasmoides pneumoniae
3.6.4.10 chaperone protein ClpB SwissProt Enterococcus faecalis
3.6.4.10 chaperone protein ClpB UniProt Francisella tularensis
3.6.4.10 chaperone protein ClpB UniProt Leptospira interrogans
3.6.4.10 chaperone protein ClpB UniProt Listeria monocytogenes
3.6.4.10 chaperone protein ClpB SwissProt Mycobacterium tuberculosis
3.6.4.10 chaperone protein ClpB UniProt Porphyromonas gingivalis
3.6.4.10 chaperone protein ClpB UniProt Staphylococcus aureus
3.6.4.10 chaperone protein ClpB SwissProt Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 chaperone protein ClpB UniProt Escherichia coli
3.6.4.10 chaperone protein ClpB UniProt Ehrlichia chaffeensis
3.6.4.10 ClpB
-
 Enterococcus faecalis
3.6.4.10 ClpB
-
 Francisella tularensis
3.6.4.10 ClpB
-
 Leptospira interrogans
3.6.4.10 ClpB
-
 Listeria monocytogenes
3.6.4.10 ClpB
-
 Mycobacterium tuberculosis
3.6.4.10 ClpB
-
 Mycoplasmoides pneumoniae
3.6.4.10 ClpB
-
 Porphyromonas gingivalis
3.6.4.10 ClpB
-
 Staphylococcus aureus
3.6.4.10 ClpB
-
 Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 ClpB
-
 Escherichia coli
3.6.4.10 ClpB
-
 Ehrlichia chaffeensis
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Enterococcus faecalis
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Francisella tularensis
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Leptospira interrogans
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Listeria monocytogenes
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Mycobacterium tuberculosis
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Mycoplasmoides pneumoniae
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Porphyromonas gingivalis
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Staphylococcus aureus
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Escherichia coli
3.6.4.10 Hsp100 molecular chaperone ClpB
-
 Ehrlichia chaffeensis

General Information

EC Number General Information Comment Organism
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Enterococcus faecalis
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Francisella tularensis
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Leptospira interrogans
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Listeria monocytogenes
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Mycobacterium tuberculosis
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Mycoplasmoides pneumoniae
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Porphyromonas gingivalis
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Staphylococcus aureus
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Escherichia coli
3.6.4.10 evolution the molecular chaperone ClpB belongs to the Hsp100/Clp subfamily of the AAA+ ATPases Ehrlichia chaffeensis
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Enterococcus faecalis
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Francisella tularensis
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Leptospira interrogans
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Listeria monocytogenes
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Mycobacterium tuberculosis
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Mycoplasmoides pneumoniae
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Porphyromonas gingivalis
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Staphylococcus aureus
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Escherichia coli
3.6.4.10 metabolism cooperation of ClpB and DnaK during aggregate reactivation Ehrlichia chaffeensis
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Enterococcus faecalis
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection. ClpB is required for survival under stress conditions and intracellular proliferation in in vitro and in vivo models Francisella tularensis
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Leptospira interrogans
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Listeria monocytogenes
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Mycobacterium tuberculosis
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Mycoplasmoides pneumoniae
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection. ClpB is required for survival under stress conditions and intracellular proliferation in in vitro and in vivo models Porphyromonas gingivalis
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection. ClpB is required for survival under stress conditions and intracellular proliferation in in vitro and in vivo models Staphylococcus aureus
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Salmonella enterica subsp. enterica serovar Typhimurium
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Escherichia coli
3.6.4.10 physiological function chaperone ClpB has a biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. ClpB disaggregates and reactivates aggregated cellular proteins. ClpB's protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection Ehrlichia chaffeensis