IED ID | IndEnz0002013436 |
Enzyme Type ID | protease013436 |
Protein Name |
Serine protease Rv3671c EC 3.4.21.- |
Gene Name | Rv3671c |
Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Enzyme Sequence | MTPSQWLDIAVLAVAFIAAISGWRAGALGSMLSFGGVLLGATAGVLLAPHIVSQISAPRAKLFAALFLILALVVVGEVAGVVLGRAVRGAIRNRPIRLIDSVIGVGVQLVVVLTAAWLLAMPLTQSKEQPELAAAVKGSRVLARVNEAAPTWLKTVPKRLSALLNTSGLPAVLEPFSRTPVIPVASPDPALVNNPVVAATEPSVVKIRSLAPRCQKVLEGTGFVISPDRVMTNAHVVAGSNNVTVYAGDKPFEATVVSYDPSVDVAILAVPHLPPPPLVFAAEPAKTGADVVVLGYPGGGNFTATPARIREAIRLSGPDIYGDPEPVTRDVYTIRADVEQGDSGGPLIDLNGQVLGVVFGAAIDDAETGFVLTAGEVAGQLAKIGATQPVGTGACVS |
Enzyme Length | 397 |
Uniprot Accession Number | P9WHR9 |
Absorption | |
Active Site | ACT_SITE 235; /note=Proton acceptor; /evidence=ECO:0000255; ACT_SITE 264; /evidence=ECO:0000255; ACT_SITE 343; /evidence=ECO:0000255 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by reducing agents and activated during exposure to oxidative stress. {ECO:0000269|PubMed:20947023}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Required for M.tuberculosis resistance to oxidative stress in addition to its role in resistance to acid, which is essential for virulence. It protects M.tuberculosis against phagolysosomal concentrations of acid and maintains its intrabacterial pH when phagocytosed by IFN-gamma-activated macrophages. {ECO:0000269|PubMed:18641659, ECO:0000269|PubMed:20947023}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Helix (9); Mutagenesis (3); Site (1); Transmembrane (4); Turn (2) |
Keywords | 3D-structure;Autocatalytic cleavage;Disulfide bond;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: Autocleaved. The autocleavage activity is significant only when no reducing agent is present in buffers. |
Signal Peptide | |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 3K6Y; 3K6Z; 3LT3; |
Mapped Pubmed ID | 28057704; |
Motif | |
Gene Encoded By | |
Mass | 40,721 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |