Detail Information for IndEnz0009000151
IED ID IndEnz0009000151
Enzyme Type ID chitinase000151
Protein Name Type II secretion system core protein G
T2SS core protein G
Protein transport protein HofG
Putative general secretion pathway protein G
Gene Name gspG hofG hopG b3328 JW3290
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MRATDKQRGFTLLEIMVVIVIIGVLASLVVPNLMGNKEKADKQKAVSDIVALENALDMYKLDNHHYPTTNQGLESLVEAPTLPPLAANYNKEGYIKRLPADPWGNDYVLVNPGEHGAYDLLSAGPDGEMGTEDDITNWGLSKKKK
Enzyme Length 145
Uniprot Accession Number P41442
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth. {ECO:0000250|UniProtKB:Q00514}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Modified residue (1); Propeptide (1); Region (1); Transmembrane (1)
Keywords Cell inner membrane;Cell membrane;Membrane;Methylation;Protein transport;Reference proteome;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:Q00514}; Single-pass membrane protein {ECO:0000255}.
Modified Residue MOD_RES 10; /note=N-methylphenylalanine; /evidence=ECO:0000255|PROSITE-ProRule:PRU01070
Post Translational Modification PTM: Cleaved by the prepilin peptidase. {ECO:0000250|UniProtKB:Q00514}.; PTM: Methylated by prepilin peptidase at the amino group of the N-terminal phenylalanine once the leader sequence is cleaved. {ECO:0000250|UniProtKB:Q00514}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 15,905
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda