TSE3_PSEAE
ID TSE3_PSEAE Reviewed; 408 AA.
AC Q9HYC5;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Peptidoglycan muramidase Tse3 {ECO:0000303|PubMed:21776080};
DE AltName: Full=Toxin Tse3;
DE EC=3.2.1.17;
GN Name=tse3 {ECO:0000303|PubMed:21776080}; OrderedLocusNames=PA3484;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-250, AND CATALYTIC
RP ACTIVITY.
RX PubMed=21776080; DOI=10.1038/nature10244;
RA Russell A.B., Hood R.D., Bui N.K., LeRoux M., Vollmer W., Mougous J.D.;
RT "Type VI secretion delivers bacteriolytic effectors to target cells.";
RL Nature 475:343-347(2011).
RN [3] {ECO:0007744|PDB:4LUQ}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION,
RP AND COFACTOR.
RX PubMed=24025333; DOI=10.1074/jbc.c113.506097;
RA Li L., Zhang W., Liu Q., Gao Y., Gao Y., Wang Y., Wang D.Z., Li Z.,
RA Wang T.;
RT "Structural Insights on the bacteriolytic and self-protection mechanism of
RT muramidase effector Tse3 in Pseudomonas aeruginosa.";
RL J. Biol. Chem. 288:30607-30613(2013).
RN [4] {ECO:0007744|PDB:4M5E, ECO:0007744|PDB:4M5F, ECO:0007744|PDB:4N7S}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 1-402 IN COMPLEX WITH CALCIUM,
RP COFACTOR, INTERACTION WITH TSI3, AND MUTAGENESIS OF ASP-18; GLU-25; GLU-250
RP AND ASP-262.
RX PubMed=24724564; DOI=10.1111/mmi.12616;
RA Lu D., Shang G., Zhang H., Yu Q., Cong X., Yuan J., He F., Zhu C., Zhao Y.,
RA Yin K., Chen Y., Hu J., Zhang X., Yuan Z., Xu S., Hu W., Cang H., Gu L.;
RT "Structural insights into the T6SS effector protein Tse3 and the Tse3-Tsi3
RT complex from Pseudomonas aeruginosa reveal a calcium-dependent membrane-
RT binding mechanism.";
RL Mol. Microbiol. 92:1092-1112(2014).
CC -!- FUNCTION: Toxin secreted by the H1 type VI (H1-T6SS) secretion system
CC into the periplasm of recipient cells. Degrades peptidoglycan via
CC muramidase activity thereby helping itself to compete with other
CC bacteria (PubMed:21776080). To protect itself, the bacterium
CC synthesizes immunity protein Tsi3 that specifically interacts with and
CC inactivates cognate toxin (PubMed:24025333).
CC {ECO:0000269|PubMed:21776080, ECO:0000269|PubMed:24025333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000269|PubMed:21776080};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:24025333};
CC -!- ACTIVITY REGULATION: Enzymatic activity depends on membrane binding.
CC {ECO:0000269|PubMed:24724564}.
CC -!- SUBUNIT: Forms an heterotetramer with Tsi3 consisting of two Tse3
CC dimers and two Tsi3 dimers. Formation of the complex inactivates Tse3
CC enzymatic activity. {ECO:0000269|PubMed:24025333,
CC ECO:0000269|PubMed:24724564}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000269|PubMed:21776080}.
CC Secreted {ECO:0000269|PubMed:21776080}. Note=Delivered to the target
CC cell periplasm by the H1 type VI (H1-T6SS) secretion system.
CC {ECO:0000269|PubMed:21776080}.
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DR EMBL; AE004091; AAG06872.1; -; Genomic_DNA.
DR PIR; E83210; E83210.
DR RefSeq; NP_252174.1; NC_002516.2.
DR RefSeq; WP_003092026.1; NZ_QZGE01000039.1.
DR PDB; 3WA5; X-ray; 1.90 A; A=1-408.
DR PDB; 4LUQ; X-ray; 1.77 A; A/B=1-408.
DR PDB; 4M5E; X-ray; 1.49 A; A=1-402.
DR PDB; 4M5F; X-ray; 2.50 A; A=1-400.
DR PDB; 4N7S; X-ray; 2.10 A; A/C=2-402.
DR PDB; 4N80; X-ray; 2.40 A; A=2-400.
DR PDB; 4N88; X-ray; 2.80 A; A/C=2-402.
DR PDBsum; 3WA5; -.
DR PDBsum; 4LUQ; -.
DR PDBsum; 4M5E; -.
DR PDBsum; 4M5F; -.
DR PDBsum; 4N7S; -.
DR PDBsum; 4N80; -.
DR PDBsum; 4N88; -.
DR AlphaFoldDB; Q9HYC5; -.
DR SMR; Q9HYC5; -.
DR STRING; 287.DR97_4437; -.
DR PaxDb; Q9HYC5; -.
DR EnsemblBacteria; AAG06872; AAG06872; PA3484.
DR GeneID; 880027; -.
DR KEGG; pae:PA3484; -.
DR PATRIC; fig|208964.12.peg.3647; -.
DR PseudoCAP; PA3484; -.
DR HOGENOM; CLU_054752_0_0_6; -.
DR OMA; SAFPTID; -.
DR BioCyc; PAER208964:G1FZ6-3552-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003796; F:lysozyme activity; IDA:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Host membrane; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..408
FT /note="Peptidoglycan muramidase Tse3"
FT /id="PRO_0000449041"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24724564,
FT ECO:0007744|PDB:4M5E"
FT MUTAGEN 18
FT /note="D->A: Significant loss of membrane-binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:24724564"
FT MUTAGEN 25
FT /note="E->A: Significant loss of membrane-binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:24724564"
FT MUTAGEN 250
FT /note="E->Q: Displays significant diminished activity."
FT /evidence="ECO:0000269|PubMed:21776080,
FT ECO:0000269|PubMed:24724564"
FT MUTAGEN 262
FT /note="D->A: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24724564"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:4M5E"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4M5F"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:4M5E"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3WA5"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4M5E"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:4N80"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:4M5E"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4M5E"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:4M5E"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:4M5E"
FT TURN 289..295
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:4M5E"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:4M5E"
SQ SEQUENCE 408 AA; 44394 MW; 05001D548AB2F35C CRC64;
MTATSDLIES LISYSWDDWQ VTRQEARRVI AAIRNDNVPD ATIAALDKSG SLIKLFQRVG
PPELARSLIA SIAGRTTMQR YQARNALIRS LINNPLGTQT DNWIYFPTIT FFDICADLAD
AAGRLGFAAA GATGVASQAI QGPFSGVGAT GVNPTDLPSI AFGDQLKLLN KDPATVTKYS
NPLGDLGAYL SQLSPQDKLN QAQTLVGQPI STLFPDAYPG NPPSRAKVMS AAARKYDLTP
QLIGAIILAE QRDQTRDEDA KDYQAAVSIK SANTSIGLGQ VVVSTAIKYE LFTDLLGQPV
RRGLSRKAVA TLLASDEFNI FATARYIRYV ANLASQQDLR KLPKTRGAFP SIDLRAYAGN
PRNWPRDNVR ALASEYTSRP WDDNLSPGWP MFVDDAYATF LDPGMRFP
