ESTA_PSEAE
ID ESTA_PSEAE Reviewed; 646 AA.
AC O33407; Q7DC45; Q9F3Y2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Esterase EstA;
DE EC=3.1.1.1 {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:20931591};
DE AltName: Full=Autotransporter esterase EstA;
DE Flags: Precursor;
GN Name=estA; Synonyms=papA; OrderedLocusNames=PA5112;
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], CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10559163; DOI=10.1128/jb.181.22.6977-6986.1999;
RA Wilhelm S., Tommassen J., Jaeger K.-E.;
RT "A novel lipolytic enzyme located in the outer membrane of Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 181:6977-6986(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Henderson I.R., Nataro J.P., Cappello R., Stein C.;
RT "Evolutionary origins of the autotransporter proteins.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP SER-38, AND OVEREXPRESSION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17631636; DOI=10.1128/jb.00023-07;
RA Wilhelm S., Gdynia A., Tielen P., Rosenau F., Jaeger K.E.;
RT "The autotransporter esterase EstA of Pseudomonas aeruginosa is required
RT for rhamnolipid production, cell motility, and biofilm formation.";
RL J. Bacteriol. 189:6695-6703(2007).
RN [5]
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).
RN [6]
RP OVEREXPRESSION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=28837648; DOI=10.1371/journal.pone.0183857;
RA Dobler L., de Carvalho B.R., Alves W.S., Neves B.C., Freire D.M.G.,
RA Almeida R.V.;
RT "Enhanced rhamnolipid production by Pseudomonas aeruginosa overexpressing
RT estA in a simple medium.";
RL PLoS ONE 12:E0183857-E0183857(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-646, AND DOMAIN.
RX PubMed=20060837; DOI=10.1016/j.jmb.2009.12.061;
RA van den Berg B.;
RT "Crystal structure of a full-length autotransporter.";
RL J. Mol. Biol. 396:627-633(2010).
CC -!- FUNCTION: Esterase whose enzymatic activity is required for rhamnolipid
CC production, all kinds of cell motility (swimming, swarming, and
CC twitching), and biofilm formation; the exact role of EstA in these
CC processes is unclear. In vitro, has pronounced esterase activities
CC towards p-nitrophenyl esters of short acyl chain length (C4-C6) and
CC Tween detergents. Also shows relatively high activity towards beta-
CC naphthyl butyrate, whereas its activities towards triacylglycerols and
CC acyls-CoA are negligible. {ECO:0000269|PubMed:17631636,
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:10559163, ECO:0000269|PubMed:20931591};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591};
CC Vmax=220 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate
CC {ECO:0000269|PubMed:20931591};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:10559163,
CC ECO:0000269|PubMed:17631636}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}.
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.
CC {ECO:0000269|PubMed:20060837}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene produce only marginal
CC amounts of extracellular rhamnolipids. They also show no swarming
CC motility, and both other forms of surface motility, swimming and
CC twitching, are completely absent in these mutant cells. Biofilm
CC formation is also affected. {ECO:0000269|PubMed:17631636}.
CC -!- MISCELLANEOUS: Overexpression of EstA results in an increased
CC production of rhamnolipids (PubMed:17631636). Rhamnolipid production is
CC strongly influenced by the C/N ratio of the environment. At a C/N ratio
CC of 83.2, a modified P.aeruginosa strain capable of overexpressing the
CC estA gene can produce up to 3.9 times more rhamnolipids than the wild-
CC type strain (PubMed:28837648). {ECO:0000269|PubMed:17631636,
CC ECO:0000269|PubMed:28837648}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC14200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF005091; AAB61674.1; -; Genomic_DNA.
DR EMBL; AJ277638; CAC14200.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG08497.1; -; Genomic_DNA.
DR PIR; G83006; G83006.
DR RefSeq; NP_253799.1; NC_002516.2.
DR RefSeq; WP_003115524.1; NZ_QZGE01000002.1.
DR PDB; 3KVN; X-ray; 2.50 A; A/X=25-646.
DR PDBsum; 3KVN; -.
DR AlphaFoldDB; O33407; -.
DR SMR; O33407; -.
DR STRING; 287.DR97_2466; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR TCDB; 1.B.12.5.9; the autotransporter-1 (at-1) family.
DR PaxDb; O33407; -.
DR PRIDE; O33407; -.
DR EnsemblBacteria; AAG08497; AAG08497; PA5112.
DR GeneID; 878826; -.
DR KEGG; pae:PA5112; -.
DR PATRIC; fig|208964.12.peg.5357; -.
DR PseudoCAP; PA5112; -.
DR HOGENOM; CLU_023098_5_0_6; -.
DR InParanoid; O33407; -.
DR OMA; HWIGGND; -.
DR PhylomeDB; O33407; -.
DR BioCyc; PAER208964:G1FZ6-5227-MON; -.
DR BRENDA; 3.1.1.1; 5087.
DR EvolutionaryTrace; O33407; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
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:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:PseudoCAP.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IDA:PseudoCAP.
DR GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
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; 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 PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Hydrolase; Membrane; Reference proteome;
KW Serine esterase; Signal; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..646
FT /note="Esterase EstA"
FT /id="PRO_0000017845"
FT TOPO_DOM 25..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..408
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..410
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..421
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..447
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..451
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..461
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..500
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..507
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..518
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..558
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..561
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..571
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..615
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..618
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..628
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..646
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT DOMAIN 366..646
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 310
FT /evidence="ECO:0000305"
FT ACT_SITE 313
FT /evidence="ECO:0000305"
FT MUTAGEN 38
FT /note="S->A: Loss of catalytic activity. Fails to
FT complement the estA mutant phenotypes."
FT /evidence="ECO:0000269|PubMed:17631636"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3KVN"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:3KVN"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 181..200
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3KVN"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 226..247
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:3KVN"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3KVN"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3KVN"
FT HELIX 339..361
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 372..384
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 393..407
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 409..427
FT /evidence="ECO:0007829|PDB:3KVN"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 432..449
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 452..474
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 477..498
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 507..523
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 541..574
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 602..616
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 619..630
FT /evidence="ECO:0007829|PDB:3KVN"
FT STRAND 633..645
FT /evidence="ECO:0007829|PDB:3KVN"
SQ SEQUENCE 646 AA; 69609 MW; AFF3CC4FFE25A191 CRC64;
MIRMALKPLV AACLLASLST APQAAPSPYS TLVVFGDSLS DAGQFPDPAG PAGSTSRFTN
RVGPTYQNGS GEIFGPTAPM LLGNQLGIAP GDLAASTSPV NAQQGIADGN NWAVGGYRTD
QIYDSITAAN GSLIERDNTL LRSRDGYLVD RARQGLGADP NALYYITGGG NDFLQGRILN
DVQAQQAAGR LVDSVQALQQ AGARYIVVWL LPDLGLTPAT FGGPLQPFAS QLSGTFNAEL
TAQLSQAGAN VIPLNIPLLL KEGMANPASF GLAADQNLIG TCFSGNGCTM NPTYGINGST
PDPSKLLFND SVHPTITGQR LIADYTYSLL SAPWELTLLP EMAHGTLRAY QDELRSQWQA
DWENWQNVGQ WRGFVGGGGQ RLDFDSQDSA ASGDGNGYNL TLGGSYRIDE AWRAGVAAGF
YRQKLEAGAK DSDYRMNSYM ASAFVQYQEN RWWADAALTG GYLDYDDLKR KFALGGGERS
EKGDTNGHLW AFSARLGYDI AQQADSPWHL SPFVSADYAR VEVDGYSEKG ASATALDYDD
QKRSSKRLGA GLQGKYAFGS DTQLFAEYAH EREYEDDTQD LTMSLNSLPG NRFTLEGYTP
QDHLNRVSLG FSQKLAPELS LRGGYNWRKG EDDTQQSVSL ALSLDF
