The Enzyme Database

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Accepted name: preflagellin peptidase
Reaction: Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly┼ or Lys-Gly┼, to release flagellin.
Other name(s): FlaK
Comments: An aspartic peptidase from Archaea but not bacteria. In peptidase family A24 (type IV prepilin peptidase family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Bardy, S.L. and Jarrell, K.F. FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity. FEMS Microbiol. Lett. 208 (2002) 53–59. [DOI] [PMID: 11934494]
2.  Ng, S.Y., VanDyke, D.J., Chaban, B., Wu, J., Nosaka, Y., Aizawa, S. and Jarrell, K.F. Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD. J. Bacteriol. 191 (2009) 6732–6740. [DOI] [PMID: 19717585]
3.  Hu, J., Xue, Y., Lee, S. and Ha, Y. The crystal structure of GXGD membrane protease FlaK. Nature 475 (2011) 528–531. [DOI] [PMID: 21765428]
[EC created 2011]

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