• • DRAMP ID

  • DRAMP00222

• • Peptide Name

  • Microcin E492 (MccE492; Bacteriocin)

• • Source

  • Klebsiella pneumoniae RYC492 (Gram-negative bacteria)

• • Family

  • Not found

• • Gene

  • mceA

• • Sequence

  • GETDPNTQLLNDLGNNMAWGAALGAPGGLGSAALGAAGGALQTVGQGLIDHGPVNVFIPVLIGPSWNGSGSGYNSATSSSGSGS

• • Sequence Length

  • 84

• • UniProt Entry

  • Q9Z4N4

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram-

• • Target Organism

  • • Gram-negative bacteria: Escherichia coli F (MIC=0.14 µM), Escherichia coli 363 (MIC=0.02 µM), Escherichia coli ML35p (MIC=0.14 µM), Escherichia coli GM1 (MIC=0.04 µM), Escherichia coli GM1 KP1060(MIC=0.65 µM), Escherichia coli W3110 (MIC=0.02 µM), Escherichia coli W3110-KP1344 Pms7 (MIC=0.08 µM), Escherichia coli W3110-6 (MIC=0.32 µM), Escherichia coli C600 (MIC=0.08 µM), Escherichia coli C600 pHX405 (MIC=0.16 µM), Salmonella enteritidis (MIC=0.6 µM), Salmonella typhimurium (MIC=1.2 µM).

• • Hemolytic Activity

  • • No hemolysis information or data found in the reference(s) presented in this entry

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Attachment to a siderophore ester

• • Nonterminal Modifications and Unusual Amino Acids

  • [Ref.15102848] The post-translational modification consists of a trimer of N-(2,3-dihydroxybnenzoyl)-L-serine linked via a C-glycosidic linkage to a β-D-glucose moiety, itself linked to the MccE492m Ser-84-carboxyl through an O-glycosidic bond.

• • Stereochemistry

  • L

• • Structure

  • Not found

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP00222.

DRAMP00222

• • Function

  • Channel-forming bacteriocin. Forms cation-selective channels. Active on enterobacteria, with highest activity against Escherichia coli. The unmodified protein is active against Escherichia coli and S. enteritidis. When the siderophore ester is present at Ser-99, antibacterial activity against these species is increased and activity is also detected against E. cloacae and K. pneumoniae.

• • PTM

  • The C-terminal Ser is modified by attachment to a siderophore similar to enterobactin, which can bind one atom of iron. The modification consists of an ester linkage of the serine carboxyl to O6 of a glucose which is linked by a C-glycosidic bond to the 5'-benzoyl of a linear triester of N-(2,3-dihydroxybenzoyl)serine. Presence of the siderophore ester increases the antibacterial activity of the protein.

• ·Literature 1

• • Title

  • Microcin E492 antibacterial activity: evidence for a TonB-dependent inner membrane permeabilization on Escherichia coli.

• • Pubmed ID

  • 12890026

• • Reference

  • Mol Microbiol. 2003 Aug;49(4):1031-1041.

• • Author

  • Destoumieux-Garz³n D, Thomas X, Santamaria M, Goulard C, Barth©l©my M, Boscher B, Bessin Y, Molle G, Pons AM, Letellier L, Peduzzi J, Rebuffat S.

• ·Literature 2

• • Title

  • Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.

• • Pubmed ID

  • 15102848

• • Reference

  • J Biol Chem. 2004 Jul 2;279(27):28233-28242.

• • Author

  • Thomas X, Destoumieux-Garz³n D, Peduzzi J, Afonso C, Blond A, Birlirakis N, Goulard C, Dubost L, Thai R, Tabet JC, Rebuffat S.

• ·Literature 3

• • Title

  • Microcin E492 forms ion channels in phospholipid bilayer membrane.

• • Pubmed ID

  • 7682973

• • Reference

  • FEBS Lett. 1993 Apr 26;321(2-3):145-148.

• • Author

  • Lagos R, Wilkens M, Vergara C, Cecchi X, Monasterio O.