UniProt functional annotation for Q9XA14



	UniProt functional annotation for Q9XA14

UniProt code: Q9XA14.

Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).

Taxonomy: Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.

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}.

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};

Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

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}.

Domain: The probably cytoplasmic N-terminus cannot be deleted without destabilizing the protein. {ECO:0000269|PubMed:27936128}.

Disruption phenotype: A single srtE1 deletion, has a significant delay in aerial hyphae formation when grown on minimal medium, but no delay on rich medium. Nearly wild-type levels of ChpC are attached to the cell wall. A double srtE1-srtE2 knockout grown on minimal medium has a more severe delay in aerial hyphae formation and does not make spores, on rich medium initiates aerial hyphae formation later than wild-type and does not make spores. In the double mutant no ChpC is attached to the cell wall in liquid medium, on solid minimal medium chpD, chpF (SCO2699), rdlA and nepA are transcribed poorly or not at all (with no change in chpH), while very few spore chains or rodlets are seen on the aerial hyphae. {ECO:0000269|PubMed:22296345}.

Similarity: Belongs to the bacterial sortase family. Class E subfamily. {ECO:0000305|PubMed:27936128}.

Annotations taken from UniProtKB at the EBI.


Organism:		Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
Taxonomy:		Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.



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}.


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};
Subcellular location:		Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
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}.
Domain:		The probably cytoplasmic N-terminus cannot be deleted without destabilizing the protein. {ECO:0000269\|PubMed:27936128}.
Disruption phenotype:		A single srtE1 deletion, has a significant delay in aerial hyphae formation when grown on minimal medium, but no delay on rich medium. Nearly wild-type levels of ChpC are attached to the cell wall. A double srtE1-srtE2 knockout grown on minimal medium has a more severe delay in aerial hyphae formation and does not make spores, on rich medium initiates aerial hyphae formation later than wild-type and does not make spores. In the double mutant no ChpC is attached to the cell wall in liquid medium, on solid minimal medium chpD, chpF (SCO2699), rdlA and nepA are transcribed poorly or not at all (with no change in chpH), while very few spore chains or rodlets are seen on the aerial hyphae. {ECO:0000269\|PubMed:22296345}.
Similarity:		Belongs to the bacterial sortase family. Class E subfamily. {ECO:0000305\|PubMed:27936128}.