Detail Information for IndEnz0009000172
IED ID IndEnz0009000172
Enzyme Type ID chitinase000172
Protein Name Type II secretion system protein H
T2SS minor pseudopilin H
General secretion pathway protein H
Protein transport protein HofH
Putative general secretion pathway protein H
Gene Name gspH hofH hopH b3329 JW3291
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MNQQRGFTLLEMMLVLALVAITASVVLFTYGREDVASTRARETAARFTAALELAIDRATLSGQPVGIHFSDSAWRIMVPGKTPSAWRWVPLQEDAADESQNDWDEELSIHLQPFKPDDSNQPQVVILADGQITPFSLLMANAGTGEPLLTLVCSGSWPLDQTLARDTRP
Enzyme Length 169
Uniprot Accession Number P41443
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. {ECO:0000250|UniProtKB:Q00515}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (11); Chain (1); Helix (1); Modified residue (1); Propeptide (1); Transmembrane (1); Turn (3)
Keywords 3D-structure;Cell inner membrane;Cell membrane;Membrane;Methylation;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport
Interact With P76086
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:Q00515}; Single-pass membrane protein {ECO:0000255}.
Modified Residue MOD_RES 7; /note=N-methylphenylalanine; /evidence=ECO:0000255|PROSITE-ProRule:PRU01070
Post Translational Modification PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00515}.; PTM: Methylated by prepilin peptidase at the amino group of the N-terminal phenylalanine once the leader sequence is cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00515}.
Signal Peptide
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 2KNQ;
Mapped Pubmed ID 16606699; 24561554;
Motif
Gene Encoded By
Mass 18,565
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda