Literature summary for 3.4.21.B56 extracted from

Yokoyama, H.; Matsui, E.; Hiramoto, K.; Forterre, P.; Matsui, I.
Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales (2013), Biochimie, 95, 1494-1501.

Search for more literature for 3.4.21.B56

Cloned(Commentary)

Cloned (Comment)	Organism
gene maps of the Pyrococcus horikoshii genome containing two sets of STOPP/stomatin gene pairs, i.e. PH1510 (long-STOPP)/PH1511 (p-stomatin) and PH0471 (short-STOPP)/PH0470 (p-stomatin). Recombinant expression of His-tagged full-length enzyme in Escherichia coli strain BL21-CodonPlus	Pyrococcus horikoshii

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	the local protein concentration of C-terminal region of enzyme PH1510 may be increased to promote self-assembly on the membrane surface by clustering the membrane-spanning regions (four membrane-spanning regions (residues 237-370) between protease domain 1510-N and OB-fold domain 1510-C) within the hydrophobic lipidbilayer	Pyrococcus horikoshii	16020	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
p-stomatin PH1511 + H2O	Pyrococcus horikoshii	the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138) and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O59179	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged full-length enzyme from Escherichia coli strain BL21-CodonPlus by nickel affinity and anion exchange chromatography, followed by dialysis	Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
p-stomatin PH1511 + H2O	the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138) and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511	Pyrococcus horikoshii	?	-	?

Subunits

Subunits	Comment	Organism
hexamer	molecular modeling of hexameric oligonucleotide binding domains of enzyme C-terminal region of enzyme PH1510 , inter-domain interactions and domain structure, overview	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
1510-C	-	Pyrococcus horikoshii
PH1510	-	Pyrococcus horikoshii
stomatin operon partner protein	-	Pyrococcus horikoshii
STOPP	-	Pyrococcus horikoshii

General Information

General Information	Comment	Organism
additional information	the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138). The hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and oligonucleotide binding-fold domains, molecular modeling of hexameric oligonucleotide binding domains of enzyme 1510-C, domain structure, overview. Conserved residues at the domain surface may play key roles in maintaining protein-protein interactions of enzyme and substrate	Pyrococcus horikoshii

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Release 2023.1 (January 2023)