IED ID |
IndEnz0002001249 |
Enzyme Type ID |
protease001249 |
Protein Name |
RNase adapter protein RapZ
|
Gene Name |
rapZ PMI3645 |
Organism |
Proteus mirabilis (strain HI4320) |
Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Morganellaceae
Proteus
Proteus mirabilis
Proteus mirabilis (strain HI4320)
|
Enzyme Sequence |
MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVDLLPELAKTLAERDAAAAAVSIDVRNMPESPEIFEKALESLPAEYSPQLLFLDADRNTLIRRYSDTRRLHPLSTKNLSLEMAIDTESDLLEPLRSRADLIIDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDRPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYVAEQLADYFRSRGKNVQSRHRTLEKRK |
Enzyme Length |
284 |
Uniprot Accession Number |
Q9ZA87 |
Absorption |
|
Active Site |
|
Activity Regulation |
|
Binding Site |
|
Calcium Binding |
|
catalytic Activity |
|
DNA Binding |
|
EC Number |
|
Enzyme Function |
FUNCTION: Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS. {ECO:0000255|HAMAP-Rule:MF_00636}. |
Temperature Dependency |
|
PH Dependency |
|
Pathway |
|
nucleotide Binding |
NP_BIND 8..15; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00636; NP_BIND 57..60; /note=GTP; /evidence=ECO:0000255|HAMAP-Rule:MF_00636 |
Features |
Chain (1); Nucleotide binding (2); Region (1); Sequence conflict (2) |
Keywords |
ATP-binding;GTP-binding;Nucleotide-binding;RNA-binding;Reference proteome |
Interact With |
|
Induction |
|
Subcellular Location |
|
Modified Residue |
|
Post Translational Modification |
|
Signal Peptide |
|
Structure 3D |
|
Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
|
Gene Encoded By |
|
Mass |
32,496 |
Kinetics |
|
Metal Binding |
|
Rhea ID |
|
Cross Reference Brenda |
|