| IED ID |
IndEnz0002001439 |
| Enzyme Type ID |
protease001439 |
| Protein Name |
Regulator of RpoS
|
| Gene Name |
rssB hnr sprE ychL b1235 JW1223 |
| Organism |
Escherichia coli (strain K12) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli (strain K12)
|
| Enzyme Sequence |
MTQPLVGKQILIVEDEQVFRSLLDSWFSSLGATTVLAADGVDALELLGGFTPDLMICDIAMPRMNGLKLLEHIRNRGDQTPVLVISATENMADIAKALRLGVEDVLLKPVKDLNRLREMVFACLYPSMFNSRVEEEERLFRDWDAMVDNPAAAAKLLQELQPPVQQVISHCRVNYRQLVAADKPGLVLDIAALSENDLAFYCLDVTRAGHNGVLAALLLRALFNGLLQEQLAHQNQRLPELGALLKQVNHLLRQANLPGQFPLLVGYYHRELKNLILVSAGLNATLNTGEHQVQISNGVPLGTLGNAYLNQLSQRCDAWQCQIWGTGGRLRLMLSAE |
| Enzyme Length |
337 |
| Uniprot Accession Number |
P0AEV1 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
ACTIVITY REGULATION: Under certain stress conditions, activity is inhibited by the anti-adapter proteins IraP, IraD and IraM. IraP is involved in response to phosphate stavation, IraD in response to DNA damage and IraM in response to magnesium starvation. IraD and IraM interact with inactive RssB, blocking its ability to interact with RpoS. IraP may mimic RpoS in its interaction with RssB and directly competing with RpoS for binding to RssB. {ECO:0000269|PubMed:16600914, ECO:0000269|PubMed:18383615, ECO:0000269|PubMed:24352426}. |
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| 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. In stationary phase, could also act as an anti-sigma factor and reduce the ability of RpoS to activate gene expression. Is also involved in the regulation of the mRNA polyadenylation pathway during stationary phase, probably by maintaining the association of PcnB with the degradosome. {ECO:0000255|HAMAP-Rule:MF_00958, ECO:0000269|PubMed:10672187, ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:19767441, ECO:0000269|PubMed:20472786, ECO:0000269|PubMed:8635466, ECO:0000269|PubMed:8637901}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (5); Chain (1); Domain (1); Helix (5); Modified residue (1); Mutagenesis (8); Turn (1) |
| Keywords |
3D-structure;Phosphoprotein;Reference proteome;Stress response |
| Interact With |
P39375; P75987; P0AAN9 |
| Induction |
INDUCTION: Expression is induced during stationary phase by RpoS. {ECO:0000269|PubMed:10869095}. |
| Subcellular Location |
|
| Modified Residue |
MOD_RES 58; /note="4-aspartylphosphate"; /evidence="ECO:0000255|HAMAP-Rule:MF_00958, ECO:0000269|PubMed:9515704" |
| Post Translational Modification |
PTM: Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS. {ECO:0000255|HAMAP-Rule:MF_00958, ECO:0000269|PubMed:10339606, ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:24352426, ECO:0000269|PubMed:9515704}. |
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (5) |
| Cross Reference PDB |
3EOD;
6Z4C;
6Z4E;
7L9C;
7LCM;
|
| Mapped Pubmed ID |
12912910;
16606699;
24561554;
32316259;
33599047;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
37,302 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
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| Cross Reference Brenda |
|