ID 3.4.21.107 DE peptidase Do. AN high temperature requirement protease A. AN HrtA heat shock protein. AN protease Do. CA Acts on substrates that are at least partially unfolded. The cleavage CA site P1 residue is normally between a pair of hydrophobic residues, such CA as Val-|-Val. CC -!- This serine endopeptidase is essential for the clearance of denatured CC or aggregated proteins from the inner-membrane and periplasmic space CC in Escherichia coli. CC -!- Natural substrates of the enzyme include colicin A lysis protein, CC pilin subunits and MalS from E.coli. CC -!- The enzyme has weak peptidase activity with casein and other non- CC native substrates. CC -!- The peptidase acts as a chaperone at low temperatures but switches to CC a peptidase (heat shock protein) at higher temperatures. CC -!- Molecular chaperones and peptidases control the folded state of CC proteins by recognizing hydrophobic stretches of polypeptide that CC become exposed by misfolding or unfolding. CC -!- They then bind these hydrophobic substrates to prevent aggregation or CC assist in protein refolding. CC -!- If attempts at refolding fail, then irreversibly damaged proteins are CC degraded by peptidases such as this enzyme. CC -!- Belongs to peptidase family S1B. DR P54925, DEGPL_BARHE; Q2YMX6, DEGPL_BRUA2; P0C114, DEGPL_BRUAB; DR Q8YG32, DEGPL_BRUME; P0A3Z5, DEGPL_BRUSU; O85291, DEGPL_BUCAP; DR Q89AP5, DEGPL_BUCBP; Q9PL97, DEGPL_CHLMU; Q9Z6T0, DEGPL_CHLPN; DR P18584, DEGPL_CHLTR; Q2SL36, DEGPL_HAHCH; E1V4H2, DEGPL_HALED; DR A6VUA4, DEGPL_MARMS; Q48EU9, DEGPL_PSE14; F6AA62, DEGPL_PSEF1; DR Q4KGQ4, DEGPL_PSEF5; A4XSC0, DEGPL_PSEMY; A5W8F5, DEGPL_PSEP1; DR B0KV30, DEGPL_PSEPG; B1J4D7, DEGPL_PSEPW; Q52894, DEGPL_RHIME; DR Q92JA1, DEGPL_RICCN; O05942, DEGPL_RICPR; P0C0V1, DEGP_ECO57 ; DR P0C0V0, DEGP_ECOLI ; P26982, DEGP_SALTY ; P39099, DEGQ_ECOLI ; DR P0AEE4, DEGS_ECO57 ; P0AEE3, DEGS_ECOLI ; P44947, DEGS_HAEIN ; DR D0ZY51, DEGS_SALT1 ; O06291, HTRA1_MYCTU; O34358, HTRA_BACSU ; DR Q9Z4H7, HTRA_LACHE ; Q9LA06, HTRA_LACLA ; A2RNT9, HTRA_LACLM ; DR Q9R9I1, HTRB_BACSU ; O53896, PEPD_MYCTU ; //