TSE1_PSEAE
ID TSE1_PSEAE Reviewed; 154 AA.
AC Q9I2Q1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Peptidoglycan amidase Tse1 {ECO:0000303|PubMed:21776080};
DE EC=3.4.19.11 {ECO:0000269|PubMed:21776080, ECO:0000269|PubMed:22700987, ECO:0000269|PubMed:22813741, ECO:0000269|PubMed:22931054};
DE AltName: Full=Type VI secretion exported 1;
GN Name=tse1 {ECO:0000303|PubMed:21776080}; OrderedLocusNames=PA1844;
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, MUTAGENESIS OF CYS-30, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
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:4EQ8, ECO:0007744|PDB:4EQA}
RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS), DISULFIDE BONDS, INTERACTION WITH
RP TSI1, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF CYS-30; HIS-91 AND
RP CYS-110, AND FUNCTION.
RX PubMed=22931054; DOI=10.1042/bj20120668;
RA Shang G., Liu X., Lu D., Zhang J., Li N., Zhu C., Liu S., Yu Q., Zhao Y.,
RA Zhang H., Hu J., Cang H., Xu S., Gu L.;
RT "Structural insight into how Pseudomonas aeruginosa peptidoglycanhydrolase
RT Tse1 and its immunity protein Tsi1 function.";
RL Biochem. J. 448:201-211(2012).
RN [4] {ECO:0007744|PDB:4EOB, ECO:0007744|PDB:4F4M}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS), DISULFIDE BONDS, ACTIVE SITE,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22813741; DOI=10.1016/j.celrep.2012.05.016;
RA Chou S., Bui N.K., Russell A.B., Lexa K.W., Gardiner T.E., LeRoux M.,
RA Vollmer W., Mougous J.D.;
RT "Structure of a peptidoglycan amidase effector targeted to Gram-negative
RT bacteria by the type VI secretion system.";
RL Cell Rep. 1:656-664(2012).
RN [5] {ECO:0007744|PDB:3VPI, ECO:0007744|PDB:3VPJ}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), DISULFIDE BONDS, INTERACTION WITH
RP TSI1, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF CYS-30; HIS-91 AND
RP CYS-110, AND FUNCTION.
RX PubMed=22700987; DOI=10.1074/jbc.m112.368043;
RA Ding J., Wang W., Feng H., Zhang Y., Wang D.C.;
RT "Structural insights into the Pseudomonas aeruginosa type VI virulence
RT effector Tse1 bacteriolysis and self-protection mechanisms.";
RL J. Biol. Chem. 287:26911-26920(2012).
CC -!- FUNCTION: Toxin secreted by the H1 type VI (H1-T6SS) secretion system
CC into the periplasm of recipient cells. Degrades peptidoglycan via
CC amidase activity thereby helping itself to compete with other bacteria
CC (PubMed:21776080, PubMed:22931054, PubMed:22813741, PubMed:22700987).
CC To protect itself, the bacterium synthesizes immunity protein Tsi1 that
CC specifically interacts with and inactivates cognate toxin
CC (PubMed:21776080, PubMed:22931054, PubMed:22700987).
CC {ECO:0000269|PubMed:21776080, ECO:0000269|PubMed:22700987,
CC ECO:0000269|PubMed:22813741, ECO:0000269|PubMed:22931054}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of gamma-D-glutamyl bonds to the L-terminus
CC (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-
CC gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm.
CC It is required that the D-terminal amino and carboxy groups of meso-
CC A2pm are unsubstituted.; EC=3.4.19.11;
CC Evidence={ECO:0000269|PubMed:21776080, ECO:0000269|PubMed:22700987,
CC ECO:0000269|PubMed:22931054};
CC -!- SUBUNIT: Forms an heterotetramer with Tsi1 consisting of two Tse1
CC dimers and two Tsi1 dimers. Formation of the complex inactivates Tse1
CC enzymatic activity. {ECO:0000269|PubMed:22931054}.
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; AAG05233.1; -; Genomic_DNA.
DR PIR; F83415; F83415.
DR RefSeq; NP_250535.1; NC_002516.2.
DR RefSeq; WP_003088027.1; NZ_QZGE01000003.1.
DR PDB; 3VPI; X-ray; 1.50 A; A=1-154.
DR PDB; 3VPJ; X-ray; 2.50 A; A/B/C/D=1-154.
DR PDB; 4EOB; X-ray; 2.61 A; A/B/C/D=1-154.
DR PDB; 4EQ8; X-ray; 1.39 A; A=1-154.
DR PDB; 4EQA; X-ray; 1.60 A; A/B=6-148.
DR PDB; 4F0V; X-ray; 1.60 A; A=1-154.
DR PDB; 4F0W; X-ray; 1.24 A; A=1-154.
DR PDB; 4F4M; X-ray; 2.68 A; A/B/C/D=1-154.
DR PDB; 4FGD; X-ray; 2.60 A; A/B/C/D=1-154.
DR PDB; 4FGE; X-ray; 1.70 A; A/B/C/D=1-154.
DR PDB; 4FGI; X-ray; 3.20 A; A/C/E/G=1-154.
DR PDB; 4FQA; X-ray; 2.10 A; A=1-154.
DR PDB; 4FQB; X-ray; 2.69 A; A/C/E/G=1-154.
DR PDBsum; 3VPI; -.
DR PDBsum; 3VPJ; -.
DR PDBsum; 4EOB; -.
DR PDBsum; 4EQ8; -.
DR PDBsum; 4EQA; -.
DR PDBsum; 4F0V; -.
DR PDBsum; 4F0W; -.
DR PDBsum; 4F4M; -.
DR PDBsum; 4FGD; -.
DR PDBsum; 4FGE; -.
DR PDBsum; 4FGI; -.
DR PDBsum; 4FQA; -.
DR PDBsum; 4FQB; -.
DR AlphaFoldDB; Q9I2Q1; -.
DR SMR; Q9I2Q1; -.
DR STRING; 287.DR97_33; -.
DR PaxDb; Q9I2Q1; -.
DR DNASU; 880830; -.
DR EnsemblBacteria; AAG05233; AAG05233; PA1844.
DR GeneID; 880830; -.
DR KEGG; pae:PA1844; -.
DR PATRIC; fig|208964.12.peg.1917; -.
DR PseudoCAP; PA1844; -.
DR HOGENOM; CLU_1685041_0_0_6; -.
DR OMA; FSWTHAD; -.
DR BioCyc; PAER208964:G1FZ6-1883-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:0004040; F:amidase activity; IDA:PseudoCAP.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Host membrane; Hydrolase; Membrane;
KW Reference proteome; Secreted.
FT CHAIN 1..154
FT /note="Peptidoglycan amidase Tse1"
FT /id="PRO_0000449039"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:22813741,
FT ECO:0000269|PubMed:22931054"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:22813741,
FT ECO:0000269|PubMed:22931054"
FT DISULFID 7..148
FT /evidence="ECO:0007744|PDB:3VPI, ECO:0007744|PDB:3VPJ,
FT ECO:0007744|PDB:4EOB, ECO:0007744|PDB:4EQ8,
FT ECO:0007744|PDB:4EQA, ECO:0007744|PDB:4F0V,
FT ECO:0007744|PDB:4F0W, ECO:0007744|PDB:4F4M,
FT ECO:0007744|PDB:4FGD, ECO:0007744|PDB:4FGI,
FT ECO:0007744|PDB:4FQA, ECO:0007744|PDB:4FQB"
FT MUTAGEN 30
FT /note="C->A: Complete loss of peptidoglycan degradation."
FT /evidence="ECO:0000269|PubMed:21776080,
FT ECO:0000269|PubMed:22700987"
FT MUTAGEN 91
FT /note="H->A: Complete loss of peptidoglycan degradation."
FT /evidence="ECO:0000269|PubMed:21776080,
FT ECO:0000269|PubMed:22700987"
FT MUTAGEN 110
FT /note="C->A: No loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:22700987,
FT ECO:0000269|PubMed:22931054"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:4FGI"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4F0W"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:4F0W"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4F0W"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4F0W"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4F0W"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4F0W"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4F0W"
FT TURN 132..136
FT /evidence="ECO:0007829|PDB:4F0W"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:4F0W"
SQ SEQUENCE 154 AA; 16443 MW; 5EE633886D9D6DD7 CRC64;
MDSLDQCIVN ACKNSWDKSY LAGTPNKDNC SGFVQSVAAE LGVPMPRGNA NAMVDGLEQS
WTKLASGAEA AQKAAQGFLV IAGLKGRTYG HVAVVISGPL YRQKYPMCWC GSIAGAVGQS
QGLKSVGQVW NRTDRDRLNY YVYSLASCSL PRAS
