| IED ID | IndEnz0002003633 |
| Enzyme Type ID | protease003633 |
| Protein Name |
Protease HtpX EC 3.4.24.- Heat shock protein HtpX |
| Gene Name | htpX b1829 JW1818 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MMRIALFLLTNLAVMVVFGLVLSLTGIQSSSVQGLMIMALLFGFGGSFVSLLMSKWMALRSVGGEVIEQPRNERERWLVNTVATQARQAGIAMPQVAIYHAPDINAFATGARRDASLVAVSTGLLQNMSPDEAEAVIAHEISHIANGDMVTMTLIQGVVNTFVIFISRILAQLAAGFMGGNRDEGEESNGNPLIYFAVATVLELVFGILASIITMWFSRHREFHADAGSAKLVGREKMIAALQRLKTSYEPQEATSMMALCINGKSKSLSELFMTHPPLDKRIEALRTGEYLK |
| Enzyme Length | 293 |
| Uniprot Accession Number | P23894 |
| Absorption | |
| Active Site | ACT_SITE 140; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. {ECO:0000269|PubMed:16076848}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Mutagenesis (7); Topological domain (3); Transmembrane (2) |
| Keywords | Autocatalytic cleavage;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Stress response;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By temperature upshift (by the sigma-32 heat shock transcription factor). Also under control of CpxR. {ECO:0000269|PubMed:12081643, ECO:0000269|PubMed:1826904}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12081643}; Multi-pass membrane protein {ECO:0000269|PubMed:12081643}. Note=Bioinformatics programs predict 4 transmembrane helices, however PhoA and Bla fusions as well as other experiments only confirm the first 2. {ECO:0000269|PubMed:12081643}. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes self-cleavage. This may not be physiological. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,923 |
| Kinetics | |
| Metal Binding | METAL 139; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 143; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 222; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |