PQSE_PSEAE
ID PQSE_PSEAE Reviewed; 301 AA.
AC P20581;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=2-aminobenzoylacetyl-CoA thioesterase {ECO:0000305};
DE EC=3.1.2.32 {ECO:0000269|PubMed:25960261, ECO:0000269|PubMed:27082157};
GN Name=pqsE {ECO:0000303|PubMed:12426334}; OrderedLocusNames=PA1000;
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 [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=2153661; DOI=10.1128/jb.172.2.884-900.1990;
RA Essar D.W., Eberly L., Hadero A., Crawford I.P.;
RT "Identification and characterization of genes for a second anthranilate
RT synthase in Pseudomonas aeruginosa: interchangeability of the two
RT anthranilate synthases and evolutionary implications.";
RL J. Bacteriol. 172:884-900(1990).
RN [2]
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 [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12426334; DOI=10.1128/jb.184.23.6472-6480.2002;
RA Gallagher L.A., McKnight S.L., Kuznetsova M.S., Pesci E.C., Manoil C.;
RT "Functions required for extracellular quinolone signaling by Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 184:6472-6480(2002).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18776012; DOI=10.1128/jb.00753-08;
RA Farrow J.M. III, Sund Z.M., Ellison M.L., Wade D.S., Coleman J.P.,
RA Pesci E.C.;
RT "PqsE functions independently of PqsR-Pseudomonas quinolone signal and
RT enhances the rhl quorum-sensing system.";
RL J. Bacteriol. 190:7043-7051(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=25960261; DOI=10.1016/j.chembiol.2015.04.012;
RA Drees S.L., Fetzner S.;
RT "PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in
RT the biosynthesis of alkylquinolone signaling molecules.";
RL Chem. Biol. 22:611-618(2015).
RN [6]
RP FUNCTION.
RX PubMed=27851827; DOI=10.1371/journal.ppat.1006029;
RA Rampioni G., Falcone M., Heeb S., Frangipani E., Fletcher M.P.,
RA Dubern J.F., Visca P., Leoni L., Camara M., Williams P.;
RT "Unravelling the genome-wide contributions of specific 2-alkyl-4-quinolones
RT and PqsE to quorum sensing in Pseudomonas aeruginosa.";
RL PLoS Pathog. 12:E1006029-E1006029(2016).
RN [7] {ECO:0007744|PDB:2Q0I, ECO:0007744|PDB:2Q0J, ECO:0007744|PDB:3DH8}
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) IN COMPLEX WITH IRON, FUNCTION AS AN
RP HYDROLASE, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-182.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19788310; DOI=10.1021/bi900123j;
RA Yu S., Jensen V., Seeliger J., Feldmann I., Weber S., Schleicher E.,
RA Haussler S., Blankenfeldt W.;
RT "Structure elucidation and preliminary assessment of hydrolase activity of
RT PqsE, the Pseudomonas quinolone signal (PQS) response protein.";
RL Biochemistry 48:10298-10307(2009).
RN [8] {ECO:0007744|PDB:2VW8}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON.
RX PubMed=20419351; DOI=10.1007/s10969-010-9090-y;
RA Oke M., Carter L.G., Johnson K.A., Liu H., McMahon S.A., Yan X., Kerou M.,
RA Weikart N.D., Kadi N., Sheikh M.A., Schmelz S., Dorward M., Zawadzki M.,
RA Cozens C., Falconer H., Powers H., Overton I.M., van Niekerk C.A., Peng X.,
RA Patel P., Garrett R.A., Prangishvili D., Botting C.H., Coote P.J.,
RA Dryden D.T., Barton G.J., Schwarz-Linek U., Challis G.L., Taylor G.L.,
RA White M.F., Naismith J.H.;
RT "The Scottish Structural Proteomics Facility: targets, methods and
RT outputs.";
RL J. Struct. Funct. Genomics 11:167-180(2010).
RN [9] {ECO:0007744|PDB:5HIO, ECO:0007744|PDB:5HIP, ECO:0007744|PDB:5HIQ, ECO:0007744|PDB:5HIS}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEXES WITH IRON AND
RP INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27082157; DOI=10.1021/acschembio.6b00156;
RA Zender M., Witzgall F., Drees S.L., Weidel E., Maurer C.K., Fetzner S.,
RA Blankenfeldt W., Empting M., Hartmann R.W.;
RT "Dissecting the multiple roles of PqsE in Pseudomonas aeruginosa virulence
RT by discovery of small tool compounds.";
RL ACS Chem. Biol. 11:1755-1763(2016).
CC -!- FUNCTION: Required for the biosynthesis of the quorum-sensing signaling
CC molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-
CC quinolone (Pseudomonas quinolone signal or PQS), which are important
CC for biofilm formation and virulence. Catalyzes the hydrolysis of the
CC intermediate 2-aminobenzoylacetyl-CoA (2-ABA-CoA) to form 2-
CC aminobenzoylacetate (2-ABA), the precursor of HHQ. In vitro, can also
CC hydrolyze other substrates such as S-ethyl-acetothioacetate and
CC acetoacetyl-CoA, but is inactive against anthraniloyl-CoA, malonyl-CoA
CC and octanoyl-CoA (PubMed:25960261, PubMed:27082157). Beyond its
CC thioesterase function, is involved in the regulation of diverse genes
CC coding for key virulence determinants and biofilm development
CC (PubMed:27851827). {ECO:0000269|PubMed:25960261,
CC ECO:0000269|PubMed:27082157, ECO:0000269|PubMed:27851827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate +
CC CoA + H(+); Xref=Rhea:RHEA:49444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:131446,
CC ChEBI:CHEBI:131447; EC=3.1.2.32;
CC Evidence={ECO:0000269|PubMed:25960261, ECO:0000269|PubMed:27082157};
CC -!- ACTIVITY REGULATION: Thioesterase activity, but not pyocyanine
CC production, is inhibited by 2-(pyridin-3-yl)benzoic acid, 2-(1H-pyrrol-
CC 1-yl)benzoic acid and 3-methylthiophene-2-carboxylic acid. Compounds
CC bind to the active center. {ECO:0000269|PubMed:27082157}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 mM for S-ethyl-acetothioacetate {ECO:0000269|PubMed:25960261};
CC KM=2.5 mM for acetoacetyl-CoA {ECO:0000269|PubMed:25960261};
CC KM=0.8 mM for cysteamine-S-phosphate {ECO:0000269|PubMed:25960261};
CC KM=14 uM for S-(4-nitrobenzoyl)mercaptoethane
CC {ECO:0000269|PubMed:19788310};
CC Note=kcat is 0.85 sec(-1) with S-ethyl-acetothioacetate as substrate.
CC kcat is 0.36 sec(-1) with acetoacetyl-CoA as substrate. kcat is 0.022
CC sec(-1) with cysteamine-S-phosphate as substrate (PubMed:25960261).
CC kcat is 7.2 min(-1) with S-(4-nitrobenzoyl)mercaptoethane as
CC substrate (PubMed:19788310). {ECO:0000269|PubMed:19788310,
CC ECO:0000269|PubMed:25960261};
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in pyocyanine and rhamnolipid
CC production and fails to kill worms efficiently, but can still produce
CC PQS (PubMed:12426334, PubMed:18776012). Deletion mutant produces
CC increased levels of DHQ, resulting from intramolecular cyclization of
CC 2-ABA-CoA (PubMed:25960261). {ECO:0000269|PubMed:12426334,
CC ECO:0000269|PubMed:18776012, ECO:0000269|PubMed:25960261}.
CC -!- MISCELLANEOUS: As mutant can produce wild-type levels of PQS, it was
CC originally thought that PqsE is not involved in HHQ/PQS biosynthesis
CC (PubMed:12426334, PubMed:18776012). It was shown later that the role of
CC PqsE can be taken over to some extent by the broad-specificity
CC thioesterase TesB, explaining why the pqsE deletion mutant still
CC synthesizes HHQ and PQS (PubMed:25960261).
CC {ECO:0000269|PubMed:25960261, ECO:0000305|PubMed:12426334,
CC ECO:0000305|PubMed:18776012}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
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; M33810; AAA88447.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04389.1; -; Genomic_DNA.
DR PIR; C35116; C35116.
DR RefSeq; NP_249691.1; NC_002516.2.
DR RefSeq; WP_003086247.1; NZ_QZGE01000006.1.
DR PDB; 2Q0I; X-ray; 1.57 A; A=1-301.
DR PDB; 2Q0J; X-ray; 2.10 A; A/B=1-301.
DR PDB; 2VW8; X-ray; 1.45 A; A=1-301.
DR PDB; 3DH8; X-ray; 1.80 A; A=1-301.
DR PDB; 5HIO; X-ray; 1.90 A; A=1-301.
DR PDB; 5HIP; X-ray; 1.99 A; A=1-301.
DR PDB; 5HIQ; X-ray; 2.10 A; A=1-301.
DR PDB; 5HIS; X-ray; 1.77 A; A=1-301.
DR PDB; 7KGW; X-ray; 1.99 A; A=1-301.
DR PDB; 7KGX; X-ray; 2.00 A; A=1-301.
DR PDBsum; 2Q0I; -.
DR PDBsum; 2Q0J; -.
DR PDBsum; 2VW8; -.
DR PDBsum; 3DH8; -.
DR PDBsum; 5HIO; -.
DR PDBsum; 5HIP; -.
DR PDBsum; 5HIQ; -.
DR PDBsum; 5HIS; -.
DR PDBsum; 7KGW; -.
DR PDBsum; 7KGX; -.
DR AlphaFoldDB; P20581; -.
DR SMR; P20581; -.
DR STRING; 287.DR97_947; -.
DR DrugBank; DB07418; bis(4-nitrophenyl) hydrogen phosphate.
DR PaxDb; P20581; -.
DR PRIDE; P20581; -.
DR EnsemblBacteria; AAG04389; AAG04389; PA1000.
DR GeneID; 880721; -.
DR KEGG; pae:PA1000; -.
DR PATRIC; fig|208964.12.peg.1032; -.
DR PseudoCAP; PA1000; -.
DR HOGENOM; CLU_932776_0_0_6; -.
DR InParanoid; P20581; -.
DR OMA; MQIRTIA; -.
DR PhylomeDB; P20581; -.
DR BioCyc; MetaCyc:MON-19871; -.
DR BioCyc; PAER208964:G1FZ6-1019-MON; -.
DR BRENDA; 3.1.2.32; 5087.
DR EvolutionaryTrace; P20581; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008800; F:beta-lactamase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..301
FT /note="2-aminobenzoylacetyl-CoA thioesterase"
FT /id="PRO_0000206249"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 71
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19788310,
FT ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:27082157"
FT MUTAGEN 182
FT /note="E->A: Strong decrease in kcat with S-(4-
FT nitrobenzoyl)mercaptoethane as substrate."
FT /evidence="ECO:0000269|PubMed:19788310"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2VW8"
FT TURN 72..77
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2Q0I"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2VW8"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2VW8"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3DH8"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:2VW8"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 233..253
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:2VW8"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:2VW8"
FT HELIX 279..296
FT /evidence="ECO:0007829|PDB:2VW8"
SQ SEQUENCE 301 AA; 34306 MW; CB78E9103D8F221C CRC64;
MLRLSAPGQL DDDLCLLGDV QVPVFLLRLG EASWALVEGG ISRDAELVWA DLCRWVADPS
QVHYWLITHK HYDHCGLLPY LCPRLPNVQV LASERTCQAW KSESAVRVVE RLNRQLLRAE
QRLPEACAWD ALPVRAVADG EWLELGPRHR LQVIEAHGHS DDHVVFYDVR RRRLFCGDAL
GEFDEAEGVW RPLVFDDMEA YLESLERLQR LPTLLQLIPG HGGLLRGRLA ADGAESAYTE
CLRLCRRLLW RQSMGESLDE LSEELHRAWG GQSVDFLPGE LHLGSMRRML EILSRQALPL
D
