IED ID | IndEnz0005000541 |
Enzyme Type ID | lipase000541 |
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; |