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Information on EC 3.4.21.102 - C-terminal processing peptidase and Organism(s) Escherichia coli and UniProt Accession P23865
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3.4.21.102 C-terminal processing peptidaseSpecify your search results
Word Map
- 3.4.21.102
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krabbe
- thylakoids
-
leukodystrophy
-
globoid
-
twitcher
- psychosine
- galactosylceramide
-
photoinhibition
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oxygen-evolving
- galactocerebroside
- agriculture
- drug development
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
stromal processing peptidase, c-terminal protease, tail-specific protease, photosystem ii d1 protein, c-terminal processing protease, carboxyl-terminal processing protease, prc protein, carboxyl-terminal protease, photosystem ii protein d1, protease re, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C-terminal processing peptidase
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C-terminal processing protease
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carboxy terminal-processing proteinase
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chloroplast protein precursor processing proteinase
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CtpA gene product
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D1 preprotein-processing proteinase
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D1 protein-processing enzyme
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photosystem D1 protein precursor carboxyl-terminal processing protease
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photosystem II D1 C-terminal processing protease
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photosystem II D1 protein
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photosystem II D1 protein processing proteinase
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PRC protein
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processing peptidase
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protease Re
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proteinase CtpA
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proteinase, chloroplast protein precursor-processing
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stromal processing peptidase
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tail-specific protease
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thylakoid protein precursor processing peptidase
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Tsp protease
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
substrate recognition site is located between amino acids 206 and 334 where there is also a putative PDZ domain
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
216484-75-2
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92480-11-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
variant of the lambda repressor + H2O
?
C-terminal sequence: WVAAA, endoproteolytic cleavage
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-
?
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala + H2O
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala + Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
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-
-
?
Arc repressor + H2O
?
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C-terminal sequence: GRIGA, endoproteolyric cleavage
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-
?
cytochrome-b562-WVAAA + H2O
?
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cytochrome b562 with a C-terminal attachment, fast hydrolysis
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-
?
cytochrome-b562-WVAAK + H2O
?
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cytochrome b562 with a C-terminal attachment, no hydrolysis
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-
?
cytochrome-b562-WVAAV + H2O
?
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cytochrome b562 with a C-terminal attachment, slow hydrolysis
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-
?
cytochrome-b562-WVAGA + H2O
?
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cytochrome b562 with a C-terminal attachment, slow hydrolysis
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-
?
cytochrome-b562-WVAYA + H2O
?
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cytochrome b562 with a C-terminal attachment, fast hydrolysis
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-
?
cytochrome-b562-WVLAA + H2O
?
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cytochrome b562 with a C-terminal attachment, fast hydrolysis
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-
?
cytochrome-b562-WVQAA + H2O
?
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cytochrome b562 with a C-terminal attachment, slow hydrolysis
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-
?
variant of the lambda repressor + H2O
?
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C-terminal sequence: WVAAA, endoproteolytic cleavage
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-
?
NIpI protein + H2O
?
-
processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
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-
?
NIpI protein + H2O
?
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processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview
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-
?
Protein + H2O
?
-
endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
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-
?
Protein + H2O
?
-
endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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-
?
Protein + H2O
?
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Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NIpI protein + H2O
?
-
processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
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-
?
Protein + H2O
?
-
endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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-
?
Protein + H2O
?
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Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0044 - 0.0111
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
0.0044
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
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wild-type enzyme
0.0095
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
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mutant V229Q
0.0111
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
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mutant V229E
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
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wild-type enzyme, mutants V229Q, V229E
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75000
75000 - 80000
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the enzyme possesses an N-terminal domain, a PDZ domain and a C-terminal catalytic domain
78500
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TspH6, enzyme protein with six additional His residues at the C-terminus, sedimentation equilibrium
75000
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TspH6, enzyme protein with six additional His residues at the C-terminus, calculation from sequence of cDNA
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D369A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D441A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D441N
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D505A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
E433A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
E449A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
G375A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
G376A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H19A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H203A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H34A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H553A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H60A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
K455A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
K455R
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
R371A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
R444A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S372A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S428A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S430A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S430C
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S432A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
T452A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
V229E
-
increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
V229Q
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increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
additional information
-
deletion of N-terminal amino acids 206-660, and deletion of C-terminal amino acids 1-334, both peptides are efficiently labelled by a competitive inhibitor of the enzyme marked with photoaffinity lable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, prolonged storage, proteolytic cleavage into two fragments of 50000 and 25000 Da
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keiler, K.C.; Sauer, R.T.
Tsp protease
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
460-461
1998
Bacillus subtilis, Bartonella bacilliformis, Escherichia coli, Haemophilus influenzae, Neisseria gonorrhoeae
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Beebe, K.D.; Shin, J.N.; Peng, J.; Chaudhury, C.; Khera, J.; Pei, D.H.
Substrate recognition through a PDZ domain in tail-specific protease
Biochemistry
39
3149-3155
2000
Escherichia coli
Keiler, K.C.; Sauer, R.T.
Sequence determinants of C-terminal substrate recognition by the Tsp protease
J. Biol. Chem.
271
2589-2593
1996
Escherichia coli
Keiler, K.C.; Silber, K.R.; Downard, K.M.; Papayannopoulos, I.A.; Biemann, K.; Sauer, R.T.
C-terminal specific protein degradation: activity and substrate specificity of the Tsp protease
Protein Sci.
4
1507-1515
1995
Escherichia coli
Keiler, K.C.; Sauer, R.T.
Identification of active site residues of the Tsp protease
J. Biol. Chem.
270
28864-28868
1995
Escherichia coli (P23865)
Silber, K.R.; Keiler, K.C.; Sauer, R.T.
Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini
Proc. Natl. Acad. Sci. USA
89
295-299
1992
Escherichia coli
EXTERNAL LINKS (specific for EC-Number 3.4.21.102)
Transporter Classification Database (TCDB): 9.B.174.1.2, 9.B.174.1.1
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