Cloned (Comment) | Organism |
---|---|
ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively, operon organization | Synechocystis sp. |
sequence analysis | Lotus japonicus |
sequence analysis | Oryza sativa |
sequence analysis | Medicago truncatula |
sequence analysis | Pisum sativum |
single gene, sequence analysis, expression analysis | Arabidopsis thaliana |
Protein Variants | Comment | Organism |
---|---|---|
additional information | downregulation of the enzyme by antisense technique in transgenic plants results in many lines with lethal seedlings | Arabidopsis thaliana |
additional information | the [1-874] deletion mutant lacking the C-terminus is inactive | Pisum sativum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
apicoplast | - |
Plasmodium falciparum | 20011 | - |
chloroplast stroma | - |
Lotus japonicus | 9570 | - |
chloroplast stroma | - |
Oryza sativa | 9570 | - |
chloroplast stroma | - |
Medicago truncatula | 9570 | - |
chloroplast stroma | - |
Pisum sativum | 9570 | - |
chloroplast stroma | - |
Arabidopsis thaliana | 9570 | - |
thylakoid | - |
Chlamydomonas reinhardtii | 9579 | - |
thylakoid | - |
Anabaena sp. | 9579 | - |
thylakoid | - |
Synechocystis sp. | 9579 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Chlamydomonas reinhardtii | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Lotus japonicus | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Oryza sativa | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Anabaena sp. | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Synechocystis sp. | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Medicago truncatula | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Arabidopsis thaliana | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif | Plasmodium falciparum | |
Zn2+ | the enzyme contains a HXXEH zinc-binding motif, metalloendopeptidase | Pisum sativum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Arabidopsis thaliana | broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo | ? | - |
? | |
additional information | Plasmodium falciparum | broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Chlamydomonas reinhardtii | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Lotus japonicus | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Oryza sativa | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Anabaena sp. | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Synechocystis sp. | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Medicago truncatula | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
additional information | Pisum sativum | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | ? | - |
? | |
pre-LHCP protein + H2O | Pisum sativum | - |
LHCP protein + transit peptide | - |
? | |
pre-RBCS protein + H2O | Chlamydomonas reinhardtii | - |
RBCS protein + transit peptide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Anabaena sp. | - |
strain PCC 7120, ORF ALL1021 | - |
Arabidopsis thaliana | O48870 | - |
- |
Chlamydomonas reinhardtii | - |
- |
- |
Lotus japonicus | - |
- |
- |
Medicago truncatula | - |
- |
- |
Oryza sativa | - |
- |
- |
Pisum sativum | Q40983 | metalloendopeptidase; gene psa | - |
Plasmodium falciparum | Q8MVZ1 | putative stromal processing peptidase | - |
Synechocystis sp. | - |
strain PCC 6803, ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | reaction mechanism, process model, substrate recognition, overview | Chlamydomonas reinhardtii | |
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 | reaction mechanism, process model, substrate recognition, overview | Lotus japonicus | |
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 | reaction mechanism, process model, substrate recognition, overview | Oryza sativa | |
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 | reaction mechanism, process model, substrate recognition, overview | Anabaena sp. | |
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 | reaction mechanism, process model, substrate recognition, overview | Synechocystis sp. | |
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 | reaction mechanism, process model, substrate recognition, overview | Medicago truncatula | |
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 | reaction mechanism, process model, substrate recognition, overview | Pisum sativum | |
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 | reaction mechanism, process model, substrate recognition, overview | Arabidopsis thaliana | |
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 | reaction mechanism, process model, substrate recognition, overview | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo | Arabidopsis thaliana | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Plasmodium falciparum | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Chlamydomonas reinhardtii | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Lotus japonicus | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Oryza sativa | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Anabaena sp. | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Synechocystis sp. | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Medicago truncatula | ? | - |
? | |
additional information | broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview | Pisum sativum | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Chlamydomonas reinhardtii | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Lotus japonicus | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Oryza sativa | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Anabaena sp. | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Synechocystis sp. | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Medicago truncatula | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Pisum sativum | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Arabidopsis thaliana | ? | - |
? | |
additional information | substrate recognition by specific protein-protein interaction, endoprotease activity, overview | Plasmodium falciparum | ? | - |
? | |
pre-LHCP protein + H2O | - |
Pisum sativum | LHCP protein + transit peptide | - |
? | |
pre-RBCS protein + H2O | - |
Chlamydomonas reinhardtii | RBCS protein + transit peptide | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 143000-145000, two isozymes | Pisum sativum |
Synonyms | Comment | Organism |
---|---|---|
chloroplast processing enzyme | - |
Pisum sativum |
chloroplast processing enzyme | - |
Arabidopsis thaliana |
CPE | - |
Arabidopsis thaliana |
More | the enzyme probably belongs to the M16 peptidase family | Chlamydomonas reinhardtii |
More | the enzyme probably belongs to the M16 peptidase family | Lotus japonicus |
More | the enzyme probably belongs to the M16 peptidase family | Oryza sativa |
More | the enzyme probably belongs to the M16 peptidase family | Anabaena sp. |
More | the enzyme probably belongs to the M16 peptidase family | Synechocystis sp. |
More | the enzyme probably belongs to the M16 peptidase family | Medicago truncatula |
More | the enzyme probably belongs to the M16 peptidase family | Arabidopsis thaliana |
More | the enzyme probably belongs to the M16 peptidase family | Plasmodium falciparum |
SPP | - |
Chlamydomonas reinhardtii |
SPP | - |
Lotus japonicus |
SPP | - |
Oryza sativa |
SPP | - |
Anabaena sp. |
SPP | - |
Synechocystis sp. |
SPP | - |
Medicago truncatula |
SPP | - |
Pisum sativum |
SPP | - |
Arabidopsis thaliana |
SPP | - |
Plasmodium falciparum |
stromal processing peptidase | - |
Chlamydomonas reinhardtii |
stromal processing peptidase | - |
Lotus japonicus |
stromal processing peptidase | - |
Oryza sativa |
stromal processing peptidase | - |
Anabaena sp. |
stromal processing peptidase | - |
Synechocystis sp. |
stromal processing peptidase | - |
Medicago truncatula |
stromal processing peptidase | - |
Pisum sativum |
stromal processing peptidase | - |
Arabidopsis thaliana |
stromal processing peptidase | - |
Plasmodium falciparum |