estB

Esterase EstB

392 amino acids

Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed.

Belongs to the class-A beta-lactamase family.

41.707 kDa

MTAASLDPTAFSLDAASLAARLDAVFDQALRERRLVGAVAIVARHGEILYRRAQGLADREAGRPMREDTLFRLASVTKPIVALAVLRLVARGELALDAPVTRWLPEFRPRLADGSEPLVTIHHLLTHTSGLGYWLLEGAGSVYDRLGISDGIDLRDFDLDENLRRLASAPLSFAPGSGWQYSLALDVLGAVVERATGQPLAAAVDALVAQPLGMRDCGFVSAEPERFAVPYHDGQPEPVRMRDGIEVPLPEGHGAAVRFAPSRVFEPGAYPSGGAGMYGSADDVLRALEAIRANPGFLPETLADAARRDQAGVGAETRGPGWGFGYLSAVLDDPAAAGTPQHAGTLQWGGVYGHSWFVDRALGLSVLLLTNTAYEGMSGPLTIALRDAVYAR

estB

Siderophore triacetylfusarinine C esterase

292 amino acids

Displays specific TAFC esterase activity but does not hydrolyze fusarinine C, which has the same core structure as TAFC (PubMed:17586718). Hydrolysis optimizes but is not essential for TAFC-mediated iron uptake (PubMed:17586718).Both extra- and intracellular siderophores have been shown to be crucial for the virulence (PubMed:17586718). Subsequent to chelation of iron and uptake, FsC and TAFC are hydrolyzed and the iron is transferred to the metabolism or to the intracellular siderophore ferricrocin (FC) for transport and storage of iron (PubMed:17586718). Hydrolyzes both TAFC and DF-TAFC with equal efficiencies, suggesting that its function might not be restricted to the release of iron from the siderophore but might also include the degradation of the iron-free chelator to protect cells (PubMed:17586718).

Belongs to the esterase D family.

32.681 kDa

MGDRPTPVPLPNSEQFYLENDRGEPYLIQVSWPLHWEDKQTGRGPLPIIYIVDGNALFLTATEAAWRRAAASHFAGGGIIVAIGYPLKGKLYDARRRSFDLTPPTACAPVGYGGADVFLDFIENSVRPAVQARFPQVSLAREALYGHSYGGLLALHALFTRPQSFDCYIASSPSIWWNSLCILHEAKAFVETKKVSHDQSPSLMVSWGSWEQHPPRWADELLDHYEARKRTAAELRMADNALDLCAMLHGCSRLHALIKTEYEGEDHTSVMSCSVSRGLTMFFEDWPFHQSG

estB

Extracellular esterase EstB

210 amino acids

An esterase which preferentially hydrolyzes triacylglyceride substrates with short chain fatty acids (less than C10) with the maximum activity towards tricaprylin (C8:0). Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18.

Belongs to the AB hydrolase superfamily.

22.363 kDa

MKKVLMAFIICLSLILSVLAAPPSGAKAESVHNPVVLVHGISGASYNFFAIKNYLISQGWQSNKLYAIDFYDKTGNNLNNGPQLASYVDRVLKETGAKKVDIVAHSMGGANTLYYIKYLGGGNKIQNVVTLGGANGLVSSTALPGTDPNQKILYTSIYSLNDQIVINSLSRLQGARNIQLYGIGHIGLLSNSQVNGYIKEGLNGGGLNTN