| IED ID |
IndEnz0002001438 |
| Enzyme Type ID |
protease001438 |
| Protein Name |
Regulator of RpoS
|
| Gene Name |
rssB hnr Z2011 ECs1737 |
| Organism |
Escherichia coli O157:H7 |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli O157:H7
|
| Enzyme Sequence |
MTQPLVGKQILIVEDEQVFRSLLDSWFSSLGATTVLAADGVDALELLGGFTPDLMICDIAMPRMNGLKLLEHIRNRGDQTPVLVISATENMADIAKALRLGVEDVLLKPVKDLNRLREMVFACLYPSMFNSRVEEEERLFRDWDAMVDNPAAAAKLLQELQPPVQQVISHCRVNYRQLVAADKPGLVLDIAALSENDLAFYCLDVTRAGHNGVLAALLLRALFNGLLQEQLAHQNQRLPELGALLKQVNHLLRQANLPGQFPLLVGYYHRELKNLILVSAGLNATLNTGEHQVQISNGVPLGTLGNAYLNQLSQRCDAWQCQIWGTGGRLRLMLSAE |
| Enzyme Length |
337 |
| Uniprot Accession Number |
P0AEV2 |
| Absorption |
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| Active Site |
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| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
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| Enzyme Function |
FUNCTION: Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co-degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation. {ECO:0000255|HAMAP-Rule:MF_00958}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
|
| Features |
Chain (1); Domain (1); Modified residue (1) |
| Keywords |
Phosphoprotein;Reference proteome;Stress response |
| Interact With |
|
| Induction |
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| Subcellular Location |
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| Modified Residue |
MOD_RES 58; /note=4-aspartylphosphate; /evidence=ECO:0000255|HAMAP-Rule:MF_00958 |
| Post Translational Modification |
PTM: Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS. {ECO:0000255|HAMAP-Rule:MF_00958}. |
| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
37,302 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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