Detail Information for IndEnz0002016212
IED ID IndEnz0002016212
Enzyme Type ID protease016212
Protein Name Prepilin leader peptidase/N-methyltransferase
Includes: Leader peptidase
EC 3.4.23.43
Prepilin peptidase
; N-methyltransferase
EC 2.1.1.-
Gene Name gspO hofD hopD hopO yheC b3335 JW3297
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MTMLLPLFILVGFIADYFVNAIAYHLSPLEDKTALTFRQVLVHFRQKKYAWHDTVPLILCVAAAIACALAPFTPIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNAQYGLIDLHDAVYGAVAGYGVLWCVYWGVWLVCHKEGLGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTITTIAFGPWLALGSMINLGYLAWISY
Enzyme Length 225
Uniprot Accession Number P25960
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.; EC=3.4.23.43; Evidence={ECO:0000250|UniProtKB:P22610};
DNA Binding
EC Number 3.4.23.43; 2.1.1.-
Enzyme Function FUNCTION: Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus. {ECO:0000305|PubMed:8655552}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Sequence conflict (2); Topological domain (7); Transmembrane (6)
Keywords Cell inner membrane;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;S-adenosyl-L-methionine;Transferase;Transmembrane;Transmembrane helix;Transport
Interact With
Induction INDUCTION: Silenced by the DNA-binding protein H-NS under standard growth conditions. {ECO:0000269|PubMed:11118204}.
Subcellular Location SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P22610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22610}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,957
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda