| IED ID | IndEnz0002016011 |
| Enzyme Type ID | protease016011 |
| Protein Name |
Rhomboid protease GluP EC 3.4.21.105 Intramembrane serine protease |
| Gene Name | gluP yqgP BSU24870 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MFLLEYTYWKIAAHLVNSGYGVIQAGESDEIWLEAPDKSSHDLVRLYKHDLDFRQEMVRDIEEQAERVERVRHQLGRRRMKLLNVFFSTEAPVDDWEEIAKKTFEKGTVSVEPAIVRGTMLRDDLQAVFPSFRTEDCSEEHASFENAQMARERFLSLVLKQEEQRKTEAAVFQNGKPTFTYLFIALQILMFFLLEINGGSTNTETLVAFGAKENSLIAQGEWWRLLTPIVLHIGIAHLAFNTLALWSVGTAVERMYGSGRFLLIYLAAGITGSIASFVFSPYPSAGASGAIFGCLGALLYVALSNRKMFLRTIGTNIIVIIIINLGFGFAVSNIDNSGHIGGLIGGFFAAAALGLPKAGAFGKRLLSAVLLIALAVGFLYYGLHSPSHQESALIQQASELYQEGKYEEVTELLNGEAAQKDASADLLKILAVSDIQIGEYDQAVSLLERAVKKEPKDHASYYNLALLYAEKNELAQAEKAIQTAVKLKPKEQRYKELQRQIENNKES |
| Enzyme Length | 507 |
| Uniprot Accession Number | P54493 |
| Absorption | |
| Active Site | ACT_SITE 288; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 339; /note=Charge relay system; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by dichloroisocoumarin (DCI) and N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), but not by other serine protease inhibitors such as sulfonyl fluoride PMSF and 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF). {ECO:0000269|PubMed:15684070}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; |
| DNA Binding | |
| EC Number | 3.4.21.105 |
| Enzyme Function | FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Important for normal cell division and sporulation. May act as a glucose exporter. {ECO:0000269|PubMed:15050034, ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:15684070, ECO:0000269|PubMed:16621838}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Is more active at more active at 25 degrees Celsius than at 37 degrees Celsius. {ECO:0000269|PubMed:15684070}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (7); Chain (1); Helix (7); Mutagenesis (6); Repeat (2); Sequence conflict (4); Transmembrane (7); Turn (2) |
| Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Repeat;Serine protease;TPR repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15616571}; Multi-pass membrane protein {ECO:0000269|PubMed:15616571}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 6R0J; |
| Mapped Pubmed ID | 31930742; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,462 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.105; |