| IED ID |
IndEnz0002013121 |
| Enzyme Type ID |
protease013121 |
| Protein Name |
Cell division inhibitor SulA
|
| Gene Name |
sulA YpAngola_A3200 |
| Organism |
Yersinia pestis bv. Antiqua (strain Angola) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Yersiniaceae
Yersinia
Yersinia pseudotuberculosis complex
Yersinia pestis
Yersinia pestis bv. Antiqua (strain Angola)
|
| Enzyme Sequence |
MRTQSLKPYHANYHSLTTNDSPTRVDAPTDSGLISEFVYSENQPVVTQLLLPLLQQLSKQSRWLLWLTPQQKLSRSWLKQSGLPINKVVQLRQINPLSTVEAMEKALLTGNYSVVLGWLPELTEDDRIRLRLAAKLGNAYGFVMRPLNDTKVGSGQCATLKIHSYLYH |
| Enzyme Length |
168 |
| Uniprot Accession Number |
A9R2N0 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
|
| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| Enzyme Function |
FUNCTION: Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. {ECO:0000255|HAMAP-Rule:MF_01179}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Region (2); Site (1) |
| Keywords |
Cell cycle;Cell division;DNA damage;SOS response;Septation |
| Interact With |
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| Induction |
INDUCTION: By DNA damage, as part of the SOS response. {ECO:0000255|HAMAP-Rule:MF_01179}. |
| Subcellular Location |
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| Modified Residue |
|
| Post Translational Modification |
PTM: Is rapidly cleaved and degraded by the Lon protease once DNA damage is repaired. {ECO:0000255|HAMAP-Rule:MF_01179}. |
| 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 |
19,060 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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