ESTP_PSEPK
ID ESTP_PSEPK Reviewed; 629 AA.
AC Q88QS0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Esterase EstP;
DE EC=3.1.1.1;
DE AltName: Full=Autotransporter esterase EstP;
DE AltName: Full=Palmitoyl-CoA hydrolase;
DE EC=3.1.2.2;
DE Flags: Precursor;
GN Name=estP; OrderedLocusNames=PP_0418;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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 catalyzes the hydrolysis of p-nitrophenyl
CC esters of acyl chain lengths C4-C10 and Tween detergents. Has also a
CC pronounced thioesterase activity towards palmitoyl-coenzyme A.
CC {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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:20931591};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591};
CC Vmax=85 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate
CC {ECO:0000269|PubMed:20931591};
CC Note=The N-terminal esterase domain, when expressed alone, shows
CC activities five to ten times higher than those of the complete enzyme
CC EstP towards all tested substrates, whereas substrate affinity and
CC the activity profiles are still the same.;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: Contains a C-terminal autotransporter domain that integrates
CC into the outer membrane and enables the translocation of the catalytic
CC N-terminal domain to the bacterial cell surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE015451; AAN66048.1; -; Genomic_DNA.
DR RefSeq; NP_742584.1; NC_002947.4.
DR RefSeq; WP_010951755.1; NC_002947.4.
DR AlphaFoldDB; Q88QS0; -.
DR SMR; Q88QS0; -.
DR STRING; 160488.PP_0418; -.
DR EnsemblBacteria; AAN66048; AAN66048; PP_0418.
DR KEGG; ppu:PP_0418; -.
DR PATRIC; fig|160488.4.peg.450; -.
DR eggNOG; COG3240; Bacteria.
DR eggNOG; COG4625; Bacteria.
DR HOGENOM; CLU_023098_5_0_6; -.
DR OMA; HWIGGND; -.
DR PhylomeDB; Q88QS0; -.
DR BioCyc; PPUT160488:G1G01-455-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 2.40.128.130; -; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR017186; Lipase_autotranspt_EstA.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR PIRSF; PIRSF037375; Autotrns_EstA; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Hydrolase; Membrane; Reference proteome;
KW Serine esterase; Signal; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..629
FT /note="Esterase EstP"
FT /id="PRO_0000407316"
FT TOPO_DOM 24..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..392
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..394
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..405
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..431
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..435
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..445
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..472
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..484
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..490
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..501
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..541
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..544
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..554
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..588
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..598
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..601
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..611
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..619
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..629
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT DOMAIN 350..629
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /evidence="ECO:0000250"
FT ACT_SITE 300
FT /evidence="ECO:0000250"
SQ SEQUENCE 629 AA; 67176 MW; FA06109522D68752 CRC64;
MRKAPLLRFT LASLALACSQ ALAGPSPYST LIVFGDSLAD AGQFPDLVGG TPGARFTNRD
ADGNFAPVSP MILGGRLGVA PGDLNPSTSV GIQPDGNNWA VGGYTTQQIL DSITTTSETV
IPPGNPNAGL VLRERPGYLA NGLRADPNAL YYLTGGGNDF LQGLVNSPAD AVAAGARLAA
SAQALQQGGA RYIMVWLLPD LGQTPNFSGT PQQNPLSLLS AAFNQSLISQ LGQIDAQIIP
LNIPLLLSEA LASPSQFGLA SDQNLVGTCY SGDSCVENPV YGINGTTPDP TKLLFNDSVH
PTIAGQQLIA DYAYSILAAP WELTLLPEMA HASLRAHQDE LRNQWQTPWQ AVGQWQAFVA
SGAQDLDFDG QHSAASGDGR GYNLTVGGSY RLNDAWRLGL AGGANRQKLE AGEQDSDYKL
NSYMASAFAQ YRQDRWWADA ALTAGHLDYS DLKRTFALGV NDRSEKGDTD GEAWAMSGRL
GYNLAADTSN WQLAPFISAD YARVKVDGYD EKSGRSTALG FDDQERTSRR LGVGLLGSVQ
VLPSTRLFAE VAQEHEFEDD EQDVTMHLTS LPANDFTLTG YTPHSDLTRA SLGVSHELVA
GVHLRGNYNW RKSDELTQQG ISVGVSVDF
