A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 220.127.116.11
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|High temperature requirement protease A.|
|HrtA heat shock protein.|
|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|
- 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-
- 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.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|P54925, DEGPL_BARHE; ||Q2YMX6, DEGPL_BRUA2; ||P0C114, DEGPL_BRUAB; |
|Q8YG32, DEGPL_BRUME; ||P0A3Z5, DEGPL_BRUSU; ||O85291, DEGPL_BUCAP; |
|Q89AP5, DEGPL_BUCBP; ||Q9PL97, DEGPL_CHLMU; ||Q9Z6T0, DEGPL_CHLPN; |
|P18584, DEGPL_CHLTR; ||Q2SL36, DEGPL_HAHCH; ||E1V4H2, DEGPL_HALED; |
|A6VUA4, DEGPL_MARMS; ||Q48EU9, DEGPL_PSE14; ||F6AA62, DEGPL_PSEF1; |
|Q4KGQ4, DEGPL_PSEF5; ||A4XSC0, DEGPL_PSEMY; ||A5W8F5, DEGPL_PSEP1; |
|B0KV30, DEGPL_PSEPG; ||B1J4D7, DEGPL_PSEPW; ||Q52894, DEGPL_RHIME; |
|Q92JA1, DEGPL_RICCN; ||O05942, DEGPL_RICPR; ||P0C0V1, DEGP_ECO57; |
|P0C0V0, DEGP_ECOLI; ||P26982, DEGP_SALTY; ||P39099, DEGQ_ECOLI; |
|P0AEE4, DEGS_ECO57; ||P0AEE3, DEGS_ECOLI; ||P44947, DEGS_HAEIN; |
|D0ZY51, DEGS_SALT1; ||O34358, HTRA_BACSU; ||Q9Z4H7, HTRA_LACHE; |
|Q9LA06, HTRA_LACLA; ||A2RNT9, HTRA_LACLM; ||Q9R9I1, HTRB_BACSU; |
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.-.-.-