ID   SRTE2_STRCO             Reviewed;         253 AA.
AC   Q9XA15;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Sortase SrtE2 {ECO:0000303|PubMed:22296345};
DE            EC=3.4.22.70 {ECO:0000305|PubMed:22296345};
GN   Name=srtE2 {ECO:0000303|PubMed:22296345}; OrderedLocusNames=SCO3849;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF CYS-220.
RC   STRAIN=A3(2) / M600;
RX   PubMed=22296345; DOI=10.1111/j.1365-2958.2012.07983.x;
RA   Duong A., Capstick D.S., Di Berardo C., Findlay K.C., Hesketh A.,
RA   Hong H.J., Elliot M.A.;
RT   "Aerial development in Streptomyces coelicolor requires sortase activity.";
RL   Mol. Microbiol. 83:992-1005(2012).
CC   -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell
CC       wall. Recognizes Leu-Ala-x-Thr-Gly and Leu-Pro-x-Thr-Gly, with a
CC       preference for the former. Unlike the S.aureus sortase it cleaves not
CC       only the Thr-Gly motif but also the Ala-X bond; an Ala-Glu bond is a
CC       better substrate than the Thr-Gly motif in vitro. Among its possible
CC       substrates are the chaplins ChpA, ChpB and ChpC; this enzyme is more
CC       important for ChpC attachment than is SrtE1. A double knockout mutant
CC       of srtE1 and srtE2 shows a developmental defect in aerial hyphae
CC       formation more dramatic than that due to chaplin deletion.
CC       {ECO:0000269|PubMed:22296345}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The enzyme catalyzes a cell wall sorting reaction in which a
CC         surface protein with a sorting signal containing a LPXTG motif is
CC         cleaved between the Thr and Gly residue. The resulting threonine
CC         carboxyl end of the protein is covalently attached to a pentaglycine
CC         cross-bridge of peptidoglycan.; EC=3.4.22.70;
CC         Evidence={ECO:0000305|PubMed:22296345};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Transcribed independently of the operon's upstream,
CC       overlapping gene (SCO3851); transcribed with srtE1 over the first 72
CC       hours of growth. Part of the strE1-srtE2 operon.
CC       {ECO:0000269|PubMed:22296345}.
CC   -!- DISRUPTION PHENOTYPE: No visible growth phenotype for the single srtE2
CC       deletion, but considerably less ChpC is attached to the cell wall. A
CC       double srtE1-srtE2 knockout grown on minimal medium has a more severe
CC       delay in aerial hyphae formation than a single srtE1 knockout and does
CC       not make spores, on rich medium the double knockout initiates aerial
CC       hyphae formation later than wild-type and does not make spores. In the
CC       double mutant no ChpC is attached to the cell wall in liquid medium, on
CC       minimal medium chpD, chpF (SCO2699), rdlA and nepA are transcribed
CC       poorly or not at all (with no change in chpH), while very few spore
CC       chains or rodlets are seen on the aerial hyphae.
CC       {ECO:0000269|PubMed:22296345}.
CC   -!- SIMILARITY: Belongs to the bacterial sortase family. Class E subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL939118; CAB45216.1; -; Genomic_DNA.
DR   PIR; T36718; T36718.
DR   RefSeq; NP_628037.1; NC_003888.3.
DR   RefSeq; WP_003975085.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9XA15; -.
DR   SMR; Q9XA15; -.
DR   STRING; 100226.SCO3849; -.
DR   GeneID; 1099285; -.
DR   KEGG; sco:SCO3849; -.
DR   PATRIC; fig|100226.15.peg.3920; -.
DR   eggNOG; COG3764; Bacteria.
DR   HOGENOM; CLU_045680_5_2_11; -.
DR   InParanoid; Q9XA15; -.
DR   OMA; SLWWTNV; -.
DR   PhylomeDB; Q9XA15; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05830; Sortase_E; 1.
DR   Gene3D; 2.40.260.10; -; 1.
DR   InterPro; IPR005754; Sortase.
DR   InterPro; IPR023365; Sortase_dom-sf.
DR   InterPro; IPR042003; Sortase_E.
DR   Pfam; PF04203; Sortase; 1.
DR   SUPFAM; SSF63817; SSF63817; 1.
DR   TIGRFAMs; TIGR01076; sortase_fam; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..253
FT                   /note="Sortase SrtE2"
FT                   /id="PRO_0000445192"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000305|PubMed:22296345"
FT   MUTAGEN         220
FT                   /note="C->A: Inactive, does not complement a double srtE1-
FT                   srtE2 knockout. Significantly reduced in vitro peptide
FT                   cleavage activity."
FT                   /evidence="ECO:0000269|PubMed:22296345"
SQ   SEQUENCE   253 AA;  27645 MW;  E87132425AC34E5E CRC64;
     MAATTDTEHQ EQAGTGGRGR RRPGRIAAQA VSVLGELLIT AGLVMGLFVV YSLWWTNVVA
     DRAADKQAEK VRDDWAQDRV GGSGQDGPGA LDTKAGIGFL HVPAMSEGDI LVEKGTSMKI
     LNDGVAGYYT DPVKATLPTS DEKGNFSLAA HRDGHGARFH NIDKIEKGDP IVFETKDTWY
     VYKTYAVLPE TSKYNVEVLG GIPKESGKKK AGHYITLTTC TPVYTSRYRY VVWGELVRTE
     KVDGDRTPPK ELR