| IED ID | IndEnz0002003090 |
| Enzyme Type ID | protease003090 |
| Protein Name |
ATP-dependent zinc metalloprotease FtsH 2 EC 3.4.24.- |
| Gene Name | ftsH2 slr0228 |
| 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 | MKFSWRTALLWSLPLLVVGFFFWQGSFGGADANLGSNTANTRMTYGRFLEYVDAGRITSVDLYENGRTAIVQVSDPEVDRTLRSRVDLPTNAPELIARLRDSNIRLDSHPVRNNGMVWGFVGNLIFPVLLIASLFFLFRRSSNMPGGPGQAMNFGKSKARFQMDAKTGVMFDDVAGIDEAKEELQEVVTFLKQPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCLIFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFEGNTGIIIIAATNRPDVLDSALMRPGRFDRQVMVDAPDYSGRKEILEVHARNKKLAPEVSIDSIARRTPGFSGADLANLLNEAAILTARRRKSAITLLEIDDAVDRVVAGMEGTPLVDSKSKRLIAYHEVGHAIVGTLLKDHDPVQKVTLIPRGQAQGLTWFTPNEEQGLTTKAQLMARIAGAMGGRAAEEEVFGDDEVTTGAGGDLQQVTEMARQMVTRFGMSNLGPISLESSGGEVFLGGGLMNRSEYSEEVATRIDAQVRQLAEQGHQMARKIVQEQREVVDRLVDLLIEKETIDGEEFRQIVAEYAEVPVKEQLIPQL |
| Enzyme Length | 627 |
| Uniprot Accession Number | Q55700 |
| Absorption | |
| Active Site | ACT_SITE 434; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity). {ECO:0000250}.; FUNCTION: Plays a role in the selective replacement of photosystem II (PSII) protein D1 in the PSII repair cycle following visible-light and UV-B induced damage. If damaged D1 is not removed then new D1 cannot be inserted to restore the PSII reaction center. Seems to also degrade damaged and/or unassembled PSII proteins D2 and PsbB (CP47). May recognize D1 via its first 20 amino acids, as deletion of these prevents the PSII repair cycle. Also seems to degrade cytoplasmic GGPS, glucosylglycerol-phosphate synthase. {ECO:0000269|PubMed:12953117, ECO:0000269|PubMed:17208194}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 212..219; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (1); Chain (1); Metal binding (3); Nucleotide binding (1); Topological domain (3); Transmembrane (2) |
| Keywords | ATP-binding;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleotide-binding;Protease;Reference proteome;Thylakoid;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By UV-B light and oxidative stress provided by methyl viologen. {ECO:0000269|PubMed:17208194, ECO:0000269|PubMed:17635189}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}; Multi-pass membrane protein {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}; Stromal side {ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:12953117}. Note=A fraction is found associated with PSII. Localization to the cell inner membrane has been specifically tested and not seen. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18000013; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,496 |
| Kinetics | |
| Metal Binding | METAL 433; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 437; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 511; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B20; |