SRTE1_STRCO
ID SRTE1_STRCO Reviewed; 352 AA.
AC Q9XA14;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sortase SrtE1 {ECO:0000303|PubMed:22296345};
DE EC=3.4.22.70 {ECO:0000305|PubMed:22296345};
DE AltName: Full=Sortase E1 transpeptidase {ECO:0000303|PubMed:27936128};
GN Name=srtE1 {ECO:0000303|PubMed:22296345}; OrderedLocusNames=SCO3850;
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, POSSIBLE ACTIVE SITE, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF VAL-119 AND CYS-320.
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).
RN [3] {ECO:0007744|PDB:5CUW}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 162-352 IN COMPLEX WITH SUBSTRATE
RP ANALOG, FUNCTION, POSSIBLE ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF
RP 82-ARG--LYS-90.
RX PubMed=27936128; DOI=10.1371/journal.pone.0167763;
RA Kattke M.D., Chan A.H., Duong A., Sexton D.L., Sawaya M.R., Cascio D.,
RA Elliot M.A., Clubb R.T.;
RT "Crystal structure of the Streptomyces coelicolor sortase E1 transpeptidase
RT provides insight into the binding mode of the novel class E sorting
RT signal.";
RL PLoS ONE 11:E0167763-E0167763(2016).
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell
CC wall. Recognizes both 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; Ala-Glu and Ala-His
CC bonds are better substrates than the Thr-Gly motif in vitro
CC (PubMed:22296345, PubMed:27936128). Among its possible substrates are
CC the chaplins ChpA, ChpB and ChpC; this enzyme is less important for
CC ChpC attachment than is SrtE2. A double knockout mutant of srtE1 and
CC srtE2 shows a developmental defect in aerial hyphae formation more
CC dramatic than that due to chaplin deletion (PubMed:22296345).
CC {ECO:0000269|PubMed:22296345, ECO:0000269|PubMed:27936128}.
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 srtE2 over the first 72
CC hours of growth. Part of the strE1-srtE2 operon.
CC {ECO:0000269|PubMed:22296345}.
CC -!- DOMAIN: The probably cytoplasmic N-terminus cannot be deleted without
CC destabilizing the protein. {ECO:0000269|PubMed:27936128}.
CC -!- DISRUPTION PHENOTYPE: A single srtE1 deletion, has a significant delay
CC in aerial hyphae formation when grown on minimal medium, but no delay
CC on rich medium. Nearly wild-type levels of ChpC are attached to the
CC cell wall. A double srtE1-srtE2 knockout grown on minimal medium has a
CC more severe delay in aerial hyphae formation and does not make spores,
CC on rich medium initiates aerial hyphae formation later than wild-type
CC and does not make spores. In the double mutant no ChpC is attached to
CC the cell wall in liquid medium, on solid minimal medium chpD, chpF
CC (SCO2699), rdlA and nepA are transcribed poorly or not at all (with no
CC change in chpH), while very few spore chains or rodlets are seen on the
CC aerial hyphae. {ECO:0000269|PubMed:22296345}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class E subfamily.
CC {ECO:0000305|PubMed:27936128}.
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DR EMBL; AL939118; CAB45217.1; -; Genomic_DNA.
DR PIR; T36719; T36719.
DR RefSeq; NP_628038.1; NC_003888.3.
DR RefSeq; WP_011029270.1; NZ_VNID01000003.1.
DR PDB; 5CUW; X-ray; 1.89 A; A=162-352.
DR PDBsum; 5CUW; -.
DR AlphaFoldDB; Q9XA14; -.
DR SMR; Q9XA14; -.
DR STRING; 100226.SCO3850; -.
DR GeneID; 1099286; -.
DR KEGG; sco:SCO3850; -.
DR PATRIC; fig|100226.15.peg.3921; -.
DR eggNOG; COG3764; Bacteria.
DR HOGENOM; CLU_045680_5_2_11; -.
DR InParanoid; Q9XA14; -.
DR OMA; WTNVRAH; -.
DR PhylomeDB; Q9XA14; -.
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 3D-structure; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Sortase SrtE1"
FT /id="PRO_0000445191"
FT TOPO_DOM 1..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27936128"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..352
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27936128"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 15..79
FT /note="Required for protein stability"
FT /evidence="ECO:0000269|PubMed:27936128"
FT COMPBIAS 98..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /evidence="ECO:0000305|PubMed:27936128"
FT ACT_SITE 320
FT /evidence="ECO:0000305|PubMed:22296345,
FT ECO:0000305|PubMed:27936128"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27936128"
FT SITE 229
FT /note="Substrate recognition"
FT /evidence="ECO:0000305|PubMed:27936128"
FT MUTAGEN 82..90
FT /note="Missing: Wild-type function, restores sporulation to
FT double srtE1-srtE2 knockout."
FT /evidence="ECO:0000269|PubMed:27936128"
FT MUTAGEN 119
FT /note="V->A: No effect, this is not the start codon."
FT /evidence="ECO:0000269|PubMed:22296345"
FT MUTAGEN 320
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"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:5CUW"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:5CUW"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:5CUW"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5CUW"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:5CUW"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 276..291
FT /evidence="ECO:0007829|PDB:5CUW"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:5CUW"
FT STRAND 327..341
FT /evidence="ECO:0007829|PDB:5CUW"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5CUW"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5CUW"
SQ SEQUENCE 352 AA; 37820 MW; D1825C3F2E580711 CRC64;
MTALRPERDS GTAGDQGSSY GQPYGDSGAF GGGRYEESAA GEENRPPLLD DETVALRIPE
PPAPRTAAGT GPIGGGPDGG GRAARRKAAK RRHGRRGAPR DQAPEEEAEQ APKAPLSRVE
ARRQARARKP GAAVVASRAI GEIFITTGVL MLLFVTYQLW WTNVRAHAQA NQAASNLQDD
WANGKRSPGS FEPGQGFALL HIPKLDVVVP IAEGISSKKV LDRGMVGHYA EDGLKTAMPD
AKAGNFGLAG HRNTHGEPFR YINKLEPGDP IVVETQDKYF VYKMASILPV TSPSNVSVLD
PVPKQSGFKG PGRYITLTTC TPEFTSKYRM IVWGKMVEER PRSKGKPDAL VS
