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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.B56 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.B56 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
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.B56 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 ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.B56 Pyrococcus horikoshii O59179
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Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.B56 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.B56 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

EC Number Subunits Comment Organism
3.4.21.B56 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

EC Number Synonyms Comment Organism
3.4.21.B56 1510-C
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 Pyrococcus horikoshii
3.4.21.B56 PH1510
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 Pyrococcus horikoshii
3.4.21.B56 stomatin operon partner protein
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 Pyrococcus horikoshii
3.4.21.B56 STOPP
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 Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
3.4.21.B56 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