Proteolysis

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The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

  • MMSYN1_0516 This gene codes for a transmembrane serine-type endopeptidase, which uses serine and histidine residues to cleave peptide bonds of other transmembrane proteins.
  • EG10397 glpG encodes the GlpG protein, which is a transmembrane serine-type endopeptidase in the S54 Rhomboid family. GlpG typically cleaves its transmembrane protein substrates at an inner hydrophobic region.
  • MMSYN1 0039, EG11506 (ftsH): gene encodes protein ATP-dependent zinc metalloprotease FtsH, which plays a role in the quality control of integral membrane proteins.
  • MMSYN1_0493 The pepV gene encodes for Xaa-His dipeptidase in Mycoplasma, a protein that cleaves peptide chains. The enzyme takes proteins and splits them into smaller ones.
  • EG10698 The pepQ gene encodes for Xaa-Pro dipeptidase in E. coli, a protein that cleaves peptide chains. The enzyme takes proteins and splits them into smaller ones.
  • MMSYN1_0394 This gene encodes the lon protease, which plays a critical role in degrading and splitting apart abnormal or aggregated proteins, especially during heat shock.
  • MMSYN1_0545 This gene encodes for the clpB chaperone protein, which serves as a chaperone that assists in de-aggregating and cleaving apart bonds in abnormal and/or aggregated proteins, particularly during heat shock.
  • EG10157 This gene encodes for a clpB chaperone protein in E. Coli that identifies aggregated proteins and helps to dis-aggregate them and cleave them apart. It is especially active during times of external stress, when many proteins may become denatured and aggregated.
  • EG10542 This gene encodes for the lon protease protein in E. Coli, which works as a primary enzyme to cleave apart denatured and even certain regulatory proteins into smaller, 5-10 amino acid sequences.
  • MMSYN1 0693 is a protease of unknown function which may be related to self-immunity.
  • peptidase: This peptidase's identity is unknown but is predicted to have metallopeptidase activity.
  • pepQ pepQ in Mycoplasma mycoides encodes Xaa-Pro dipeptidase, which is a metallopeptidase that splits up dipeptides with a proline amino acid residue at the C-terminal position.
  • pepQ pepQ in E. Coli encodes Xaa-Pro dipeptidase, which is a metallopeptidase that splits up dipeptides with a proline amino acid residue at the C-terminal position.