| IED ID | IndEnz0002014985 |
| Enzyme Type ID | protease014985 |
| Protein Name |
Protease HtpX homolog EC 3.4.24.- |
| Gene Name | htpX BPUM_1241 |
| Organism | Bacillus pumilus (strain SAFR-032) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus pumilus (Bacillus mesentericus) Bacillus pumilus (strain SAFR-032) |
| Enzyme Sequence | MGKRIFLFILTNILVITTIGIVLSVISAATGVGSYIGADGRISMVALLVFSAVVGFVGSFMSLAMSRWMAKMMMGVRVLNPEKDSLTYDEQQLVDRVHRLSRAAGLSKMPEVGIYQSSEVNAFATGPSKRRSLVAVSTGLLHEMDDAAVEGVIAHEVAHVANGDMVTMTLLQGIVNTFVVFLSRIAAWIASRFVSREELVPIVHFIAVIVFQIIFSVLGSLVVFAYSRHREFHADRGGADLAGKDKMVHALRSLEAYTSRIKDDDQTAVATLKISGKRKASLFSTHPDLNERIRRLEAK |
| Enzyme Length | 299 |
| Uniprot Accession Number | A8FCF7 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence=ECO:0000255|HAMAP-Rule:MF_00188 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Transmembrane (4) |
| Keywords | Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00188}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,696 |
| Kinetics | |
| Metal Binding | METAL 155; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00188; METAL 159; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00188; METAL 231; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00188 |
| Rhea ID | |
| Cross Reference Brenda |