| IED ID | IndEnz0002010181 |
| Enzyme Type ID | protease010181 |
| Protein Name |
Sortase SrtE1 EC 3.4.22.70 Sortase E1 transpeptidase |
| Gene Name | srtE1 SCO3850 |
| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albidoflavus group Streptomyces coelicolor Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Enzyme Sequence | MTALRPERDSGTAGDQGSSYGQPYGDSGAFGGGRYEESAAGEENRPPLLDDETVALRIPEPPAPRTAAGTGPIGGGPDGGGRAARRKAAKRRHGRRGAPRDQAPEEEAEQAPKAPLSRVEARRQARARKPGAAVVASRAIGEIFITTGVLMLLFVTYQLWWTNVRAHAQANQAASNLQDDWANGKRSPGSFEPGQGFALLHIPKLDVVVPIAEGISSKKVLDRGMVGHYAEDGLKTAMPDAKAGNFGLAGHRNTHGEPFRYINKLEPGDPIVVETQDKYFVYKMASILPVTSPSNVSVLDPVPKQSGFKGPGRYITLTTCTPEFTSKYRMIVWGKMVEERPRSKGKPDALVS |
| Enzyme Length | 352 |
| Uniprot Accession Number | Q9XA14 |
| Absorption | |
| Active Site | ACT_SITE 251; /evidence="ECO:0000305|PubMed:27936128"; ACT_SITE 320; /evidence="ECO:0000305|PubMed:22296345, ECO:0000305|PubMed:27936128"; ACT_SITE 329; /note="Proton donor"; /evidence="ECO:0000305|PubMed:27936128" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.; EC=3.4.22.70; Evidence={ECO:0000305|PubMed:22296345}; |
| DNA Binding | |
| EC Number | 3.4.22.70 |
| Enzyme Function | FUNCTION: Transpeptidase that anchors surface proteins to the cell wall. Recognizes both Leu-Ala-x-Thr-Gly and Leu-Pro-x-Thr-Gly, with a preference for the former. Unlike the S.aureus sortase it cleaves not only the Thr-Gly motif but also the Ala-X bond; Ala-Glu and Ala-His bonds are better substrates than the Thr-Gly motif in vitro (PubMed:22296345, PubMed:27936128). Among its possible substrates are the chaplins ChpA, ChpB and ChpC; this enzyme is less important for ChpC attachment than is SrtE2. A double knockout mutant of srtE1 and srtE2 shows a developmental defect in aerial hyphae formation more dramatic than that due to chaplin deletion (PubMed:22296345). {ECO:0000269|PubMed:22296345, ECO:0000269|PubMed:27936128}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (10); Chain (1); Compositional bias (1); Helix (6); Mutagenesis (3); Region (2); Site (1); Topological domain (2); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Transcribed independently of the operon's upstream, overlapping gene (SCO3851); transcribed with srtE2 over the first 72 hours of growth. Part of the strE1-srtE2 operon. {ECO:0000269|PubMed:22296345}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5CUW; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,820 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |