| IED ID |
IndEnz0002009786 |
| Enzyme Type ID |
protease009786 |
| Protein Name |
Secretion monitor
|
| Gene Name |
secM srrA yacA b0097 JW5007 |
| Organism |
Escherichia coli (strain K12) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli (strain K12)
|
| Enzyme Sequence |
MSGILTRWRQFGKRYFWPHLLLGMVAASLGLPALSNAAEPNAPAKATTRNHEPSAKVNFGQLALLEANTRRPNSNYSVDYWHQHAIRTVIRHLSFAMAPQTLPVAEESLPLQAQHLALLDTLSALLTQEGTPSEKGYRIDYAHFTPQAKFSTPVWISQAQGIRAGPQRLT |
| Enzyme Length |
170 |
| Uniprot Accession Number |
P62395 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Regulates secA expression by translational coupling of the secM secA operon. Ribosomes translating the C-terminal region of secM can disrupt an RNA repressor helix that normally blocks secA translation initiation, derepressing the expression of secA. Translational pausing of secM at Pro-166 under secretion-limiting conditions increases the duration of the disruption and thus increases secA expression. This is controlled by interaction of the secM signal peptide with secA and the translocon, possibly by secA pulling the paused secM out of the ribosome. The arrest sequence (150-FXXXXWIXXXXGIRAGP-166) is sufficient to cause arrest of unrelated proteins. Elongation arrest can be alleviated by mutations in the 23S rRNA or in ribosomal protein L22. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Erroneous initiation (3); Mutagenesis (7); Signal peptide (1) |
| Keywords |
3D-structure;Cytoplasm;Periplasm;Reference proteome;Signal |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1834634}. Periplasm {ECO:0000269|PubMed:1834634}. Note=The active form is cytosolic, while the periplasmic form is rapidly degraded, mainly by the tail-specific protease. |
| Modified Residue |
|
| Post Translational Modification |
|
| Signal Peptide |
SIGNAL 1..37; /evidence=ECO:0000255 |
| Structure 3D |
NMR spectroscopy (1); Electron microscopy (1) |
| Cross Reference PDB |
2N62;
3JBV;
|
| Mapped Pubmed ID |
11477104;
11574054;
1833384;
2146254;
21464303;
24561554;
2536662;
26670735;
26926436;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
18,880 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|