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ENZYME

ENZYME entry: EC 3.4.21.107

PURL: https://purl.expasy.org/enzyme/EC/3.4.21.107
Accepted Name
peptidase Do
Alternative Name(s)
high temperature requirement protease A
HrtA heat shock protein
protease Do
Reaction catalysed
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Comment(s)
  • This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli.
  • Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli.
  • The enzyme has weak peptidase activity with casein and other non- native substrates.
  • The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures.
  • Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding.
  • They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding.
  • If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme.
  • Belongs to peptidase family S1B.
Cross-references
BRENDA3.4.21.107
EC2PDB3.4.21.107
ExplorEnz3.4.21.107
KEGG Ligand Database for Enzyme Nomenclature3.4.21.107
IUBMB Enzyme Nomenclature3.4.21.107
MEDLINEFind literature relating to 3.4.21.107
MetaCyc3.4.21.107
Rhea expert-curated reactions3.4.21.107
UniProtKB/Swiss-Prot
P54925, DEGPL_BARHEQ2YMX6, DEGPL_BRUA2P0C114, DEGPL_BRUAB
Q8YG32, DEGPL_BRUMEP0A3Z5, DEGPL_BRUSUO85291, DEGPL_BUCAP
Q89AP5, DEGPL_BUCBPQ9PL97, DEGPL_CHLMUQ9Z6T0, DEGPL_CHLPN
P18584, DEGPL_CHLTRA4XSC0, DEGPL_ECTM1Q2SL36, DEGPL_HAHCH
E1V4H2, DEGPL_HALEDA6VUA4, DEGPL_MARMSQ48EU9, DEGPL_PSE14
F6AA62, DEGPL_PSEF1Q4KGQ4, DEGPL_PSEF5A5W8F5, DEGPL_PSEP1
B0KV30, DEGPL_PSEPGB1J4D7, DEGPL_PSEPWQ52894, DEGPL_RHIME
Q92JA1, DEGPL_RICCNO05942, DEGPL_RICPRP0C0V1, DEGP_ECO57
P0C0V0, DEGP_ECOLIP26982, DEGP_SALTYP39099, DEGQ_ECOLI
P0AEE4, DEGS_ECO57P0AEE3, DEGS_ECOLIP44947, DEGS_HAEIN
D0ZY51, DEGS_SALT1O06291, HTRA1_MYCTUO34358, HTRA_BACSU
Q9Z4H7, HTRA_LACHEQ9LA06, HTRA_LACLAA2RNT9, HTRA_LACLM
Q9R9I1, HTRB_BACSUO53896, PEPD_MYCTU

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.21.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-