Detail Information for IndEnz0002016522
IED ID IndEnz0002016522
Enzyme Type ID protease016522
Protein Name Rhomboid protease AarA
EC 3.4.21.105
Intramembrane serine protease
Gene Name aarA
Organism Providencia stuartii
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Morganellaceae Providencia Providencia stuartii
Enzyme Sequence MAEQQNPFSIKSKARFSLGAIALTLTLVLLNIAVYFYQIVFASPLDSRESNLILFGANIYQLSLTGDWWRYPISMMLHSNGTHLAFNCLALFVIGIGCERAYGKFKLLAIYIISGIGAALFSAYWQYYEISNSDLWTDSTVYITIGVGASGAIMGIAAASVIYLIKVVINKPNPHPVIQRRQKYQLYNLIAMIALTLINGLQSGVDNAAHIGGAIIGALISIAYILVPHKLRVANLCITVIAASLLTMMIYLYSFSTNKHLLEEREFIYQEVYTELADANQ
Enzyme Length 281
Uniprot Accession Number P46116
Absorption
Active Site ACT_SITE 150; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 210; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000269|PubMed:21439629};
DNA Binding
EC Number 3.4.21.105
Enzyme Function FUNCTION: Rhomboid serine protease that catalyzes intramembrane proteolysis. Mediates quorum-sensing and the subsequent regulation of target genes via activation of the Tat protein export system. Catalyzes the proteolytic activation of TatA by removal of its N-terminal extension. {ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:17215357, ECO:0000269|PubMed:8051030}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Mutagenesis (2); Transmembrane (7)
Keywords Cell membrane;Hydrolase;Membrane;Protease;Serine protease;Transmembrane;Transmembrane helix
Interact With A1YH68
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:17215357}; Multi-pass membrane protein {ECO:0000269|PubMed:15616571, ECO:0000269|PubMed:17215357}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 25009246;
Motif
Gene Encoded By
Mass 31,106
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.105;