| IED ID | IndEnz0002006208 |
| Enzyme Type ID | protease006208 |
| Protein Name |
Cell shape-determining protein MreBH Actin-like MreBH protein Rod shape-determining protein MreBH |
| Gene Name | mreBH BSU14470 |
| 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 | MFQSTEIGIDLGTANILVYSKNKGIILNEPSVVAVDTTTKAVLAIGADAKNMIGKTPGKIVAVRPMKDGVIADYDMTTDLLKHIMKKAAKSIGMSFRKPNVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIISFGGVVSCHSIRIGGDQLDEDIVSFVRKKYNLLIGERTAEQVKMEIGHALIEHIPEAMEIRGRDLVTGLPKTIMLQSNEIQDAMRESLLHILEAIRATLEDCPPELSGDIVDRGVILTGGGALLNGIKEWLTEEIVVPVHVAQNPLESVAIGTGRSLEVIDKLQKAIK |
| Enzyme Length | 335 |
| Uniprot Accession Number | P39763 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:16950129, PubMed:19659933). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:16950129, PubMed:19659933). A feedback loop between cell geometry and MreBH localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreBH polymerization (PubMed:21636745, PubMed:21636744). Organizes peptidoglycan synthesis in the lateral cell wall (PubMed:19659933). Required for the localization of the cell wall hydrolase LytE into the cylindrical part of the cell wall (PubMed:16950129). {ECO:0000250|UniProtKB:P0A9X4, ECO:0000269|PubMed:16950129, ECO:0000269|PubMed:19659933, ECO:0000269|PubMed:21636744, ECO:0000269|PubMed:21636745}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 13..15; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_02207; NP_BIND 159..161; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_02207; NP_BIND 207..210; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_02207; NP_BIND 287..290; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_02207 |
| Features | Chain (1); Nucleotide binding (4) |
| Keywords | ATP-binding;Cell shape;Cytoplasm;Membrane;Nucleotide-binding;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Expression is sigma I-dependent. {ECO:0000269|PubMed:18156261}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16950129}. Membrane raft {ECO:0000269|PubMed:22882210}. Note=Membrane-associated. Colocalizes with MreB and Mbl (PubMed:16950129). Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:22882210). {ECO:0000269|PubMed:16950129, ECO:0000269|PubMed:22882210}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,687 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |