EST_PSEAE
ID EST_PSEAE Reviewed; 201 AA.
AC Q9HZY8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Esterase TesA;
DE EC=3.1.1.1;
DE Flags: Precursor;
GN Name=tesA; OrderedLocusNames=PA2856;
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP PARAMETERS.
RX PubMed=20931591; DOI=10.1002/cbic.201000398;
RA Lescic Asler I., Ivic N., Kovacic F., Schell S., Knorr J., Krauss U.,
RA Wilhelm S., Kojic-Prodic B., Jaeger K.E.;
RT "Probing enzyme promiscuity of SGNH hydrolases.";
RL ChemBioChem 11:2158-2167(2010).
CC -!- FUNCTION: Esterase that exhibits the highest activity towards Tween
CC detergents and p-nitrophenyl esters of short acyl chain length. Also
CC displays a low thioesterase activity towards palmitoyl-coenzyme A, but
CC is not active towards acetyl-coenzyme A. {ECO:0000269|PubMed:20931591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000269|PubMed:20931591};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591};
CC Vmax=37 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate
CC {ECO:0000269|PubMed:20931591};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG06244.1; -; Genomic_DNA.
DR PIR; D83288; D83288.
DR RefSeq; NP_251546.1; NC_002516.2.
DR RefSeq; WP_003114753.1; NZ_QZGE01000011.1.
DR PDB; 4JGG; X-ray; 1.90 A; A/B=1-201.
DR PDBsum; 4JGG; -.
DR AlphaFoldDB; Q9HZY8; -.
DR SMR; Q9HZY8; -.
DR STRING; 287.DR97_5085; -.
DR PaxDb; Q9HZY8; -.
DR PRIDE; Q9HZY8; -.
DR DNASU; 878554; -.
DR EnsemblBacteria; AAG06244; AAG06244; PA2856.
DR GeneID; 878554; -.
DR KEGG; pae:PA2856; -.
DR PATRIC; fig|208964.12.peg.2996; -.
DR PseudoCAP; PA2856; -.
DR HOGENOM; CLU_051180_3_0_6; -.
DR InParanoid; Q9HZY8; -.
DR OMA; MRIPPNY; -.
DR PhylomeDB; Q9HZY8; -.
DR BioCyc; PAER208964:G1FZ6-2906-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004064; F:arylesterase activity; IDA:PseudoCAP.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:PseudoCAP.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..201
FT /note="Esterase TesA"
FT /id="PRO_0000407315"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4JGG"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:4JGG"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:4JGG"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:4JGG"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:4JGG"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4JGG"
FT TURN 161..169
FT /evidence="ECO:0007829|PDB:4JGG"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4JGG"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:4JGG"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4JGG"
SQ SEQUENCE 201 AA; 21038 MW; D5FE0ACD1AAA5CFE CRC64;
MRALLLSGCL ALVLLTQQAA AQTLLVVGDS ISAALGLDTS QGWVALLQKR LADEGYDYRV
VNASISGDTS AGGLARLPAL LAEEKPALVV IELGGNDGLR GMAPAQLQQN LASMAQKARA
EGAKVLLLGI QLPPNYGPRY IEAFSRVYGA VAAQEKTALV PFFLEGVGGV QGMMQADGIH
PALAAQPRLL ENVWPTLKPL L
