Detail Information for IndEnz0002019288
IED ID IndEnz0002019288
Enzyme Type ID protease019288
Protein Name Carboxyl-terminal-processing protease
EC 3.4.21.102
CtpA
Gene Name ctpA slr0008
Organism Synechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Merismopediaceae Synechocystis unclassified Synechocystis Synechocystis sp. PCC 6803 Synechocystis sp. (strain PCC 6803 / Kazusa)
Enzyme Sequence MGKRTRRFWALAFSLLMGALIYLGNTPSALAFTEEQKLLLQSWRLVNQSYLDETFNHQNWWLLREKYVKRPLRNREETYTAIEEMLATLDEPFTRLLRPEQYGNLQVTTTGELSGVGLQININPETNQLEIMAPLAGSPAEEAGLQPHDQILAIDGVDTQTLSLDEAAARMRGPKNTKVSLEILSAGTEVPQEFTLTRQLISLSPVAAQLDDSRPGQSVGYIRLSQFSANAYKEVAHALHQLEEQGADGYILDLRNNPGGLLQAGIDIARLWLPESTIVYTVNRQGTQESFTANGEAATDRPLVVLVNQGTASASEILAGALQDNQRATLVGEKTFGKGLIQSLFELSDGAGIAVTVAKYETPQHHDIHKLGIMPDEVVEQPLISFAEITSPADVQYQAALDLLTGGVAIAHKSSSIPAMATAHKPN
Enzyme Length 427
Uniprot Accession Number Q55669
Absorption
Active Site ACT_SITE 313; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 324; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 338; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.21.102;
DNA Binding
EC Number 3.4.21.102
Enzyme Function FUNCTION: Cleavage of the 16 C-terminal residues from the D1 precursor of photosystem II (PSII). This proteolytic processing is necessary to allow the light-driven assembly of the oxygen-evolving cluster (a tetranuclear manganese), which is responsible for photosynthetic water oxidation. {ECO:0000269|PubMed:8034700}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Signal peptide (1)
Keywords Hydrolase;Protease;Reference proteome;Serine protease;Signal;Thylakoid
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cellular thylakoid lumen {ECO:0000303|PubMed:8034700}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 18000013;
Motif
Gene Encoded By
Mass 46,691
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.102;