Detail Information for IndEnz0002004451
IED ID IndEnz0002004451
Enzyme Type ID protease004451
Protein Name Translational regulator CsrA
Carbon storage regulator
Gene Name csrA rsmA
Organism Proteus mirabilis
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Morganellaceae Proteus Proteus mirabilis
Enzyme Sequence MLILTRRVGETLMIGDDVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKTQPTDNY
Enzyme Length 62
Uniprot Accession Number Q93MI1
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). {ECO:0000255|HAMAP-Rule:MF_00167}.; FUNCTION: Expression from a low-copy number plasmid has no effect on swimming, but blocks swarming and virulence factor expression as measured by cell lengthening and hemolysin, protease, urease and flagellin production (PubMed:12488561). Expression destabilizes hemolysin mRNA (PubMed:12488561). Complements an E.coli disruption mutant (PubMed:12488561). {ECO:0000269|PubMed:12488561}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1)
Keywords Activator;Cytoplasm;RNA-binding;Repressor;Translation regulation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 6,981
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda