Detail Information for IndEnz0010000012
IED ID IndEnz0010000012
Enzyme Type ID esterase000012
Protein Name Esterase EstA
EC 3.1.1.1
Autotransporter esterase EstA
Gene Name estA papA PA5112
Organism Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Enzyme Sequence MIRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPMLLGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIERDNTLLRSRDGYLVDRARQGLGADPNALYYITGGGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITGQRLIADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDLKRKFALGGGERSEKGDTNGHLWAFSARLGYDIAQQADSPWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQLFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLALSLDF
Enzyme Length 646
Uniprot Accession Number O33407
Absorption
Active Site ACT_SITE 38; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 310; /evidence=ECO:0000305; ACT_SITE 313; /evidence=ECO:0000305
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:20931591};
DNA Binding
EC Number 3.1.1.1
Enzyme Function FUNCTION: Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta-naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. {ECO:0000269|PubMed:17631636, ECO:0000269|PubMed:20931591}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (25); Chain (1); Domain (1); Erroneous initiation (1); Helix (15); Mutagenesis (1); Signal peptide (1); Topological domain (11); Transmembrane (11); Turn (6)
Keywords 3D-structure;Cell outer membrane;Hydrolase;Membrane;Reference proteome;Serine esterase;Signal;Transmembrane;Transmembrane beta strand
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}; Multi-pass membrane protein {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3KVN;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 69,609
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591}; Vmax=220 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate {ECO:0000269|PubMed:20931591};
Metal Binding
Rhea ID RHEA:21164
Cross Reference Brenda 3.1.1.1;