UniProt functional annotation for P25156



	UniProt functional annotation for P25156

UniProt code: P25156.

Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165).

Taxonomy: Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; Thermoplasmataceae; Thermoplasma.

Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin- like activities. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:8999862}.

Activity regulation: The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close- gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:17803938, ECO:0000269|PubMed:20360109}.

Biophysicochemical properties: Kinetic parameters: KM=39 uM for Suc-LLVY-Amc (at 55 degrees Celsius) {ECO:0000269|PubMed:8999862}; Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius) {ECO:0000269|PubMed:8999862};

Subunit: The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:1373380, ECO:0000269|PubMed:15916965, ECO:0000269|PubMed:16337593, ECO:0000269|PubMed:19889631, ECO:0000269|PubMed:20019667, ECO:0000269|PubMed:7725097}.

Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.

Ptm: The N-terminus is blocked.

Miscellaneous: The configuration of the closed gate contains an opening large enough to allow rapid entry of tetrapeptides but able to impede the entry of proteins and longer peptides.

Similarity: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP- Rule:MF_00289}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165).
Taxonomy:		Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; Thermoplasmataceae; Thermoplasma.



Function:		Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin- like activities. {ECO:0000255\|HAMAP-Rule:MF_00289, ECO:0000269\|PubMed:8999862}.


Activity regulation:		The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close- gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity. {ECO:0000255\|HAMAP-Rule:MF_00289, ECO:0000269\|PubMed:17803938, ECO:0000269\|PubMed:20360109}.
Biophysicochemical properties:		Kinetic parameters: KM=39 uM for Suc-LLVY-Amc (at 55 degrees Celsius) {ECO:0000269\|PubMed:8999862}; Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius) {ECO:0000269\|PubMed:8999862};
Subunit:		The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN. {ECO:0000255\|HAMAP-Rule:MF_00289, ECO:0000269\|PubMed:1373380, ECO:0000269\|PubMed:15916965, ECO:0000269\|PubMed:16337593, ECO:0000269\|PubMed:19889631, ECO:0000269\|PubMed:20019667, ECO:0000269\|PubMed:7725097}.
Subcellular location:		Cytoplasm {ECO:0000255\|HAMAP-Rule:MF_00289}.
Ptm:		The N-terminus is blocked.
Miscellaneous:		The configuration of the closed gate contains an opening large enough to allow rapid entry of tetrapeptides but able to impede the entry of proteins and longer peptides.
Similarity:		Belongs to the peptidase T1A family. {ECO:0000255\|HAMAP- Rule:MF_00289}.