IED ID | IndEnz0002005169 |
Enzyme Type ID | protease005169 |
Protein Name |
Putative beta-barrel assembly-enhancing protease EC 3.4.-.- |
Gene Name | VC_2164 |
Organism | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio cholerae Vibrio cholerae O1 Vibrio cholerae O1 biovar El Tor Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
Enzyme Sequence | MKFFPTRTLLCLCIAAPCLPAIAQNDPIELPDIGTVAGSTLTIDQELIYGDAYMRMLRNNQPVINDPVLNEYIDNLGHRLVASANDVKTPFTFFMIRDRNINAFAFFGGYVALHSGLFLHAQSESELASVMAHEIAHVTQRHLARSMEEQARRSPATIAALAGSLLLAIAAPEAGIAAINATMAGSIQGQINYTRSNEKEADRFGIATLAKAGFDANAMPQFFTRLADEYRYASKPPPMLLTHPLPEDRITDSRERARQYPPLKLAPHLDYHLARARIIARYAGIDADAALDWFARSEKKIDATLQPSIQYGKALVYLDLKQFDKAEPLLTQLVKEQPDNHFYLDAISDLYIELKQADKAQSLLEKALKQTPNNSVLTINYANVLLKQDKFTDAIRILQRYTHDNPNDINGWQLLSEANSRLGNSAEDLAARGEIMALQANWNKAIQFYTQASQLVELGSLAQARYDARIDQLMVQRERFLSLQ |
Enzyme Length | 484 |
Uniprot Accession Number | Q9KQ40 |
Absorption | |
Active Site | ACT_SITE 134; /evidence=ECO:0000255|HAMAP-Rule:MF_00997; ACT_SITE 202; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_00997 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.-.- |
Enzyme Function | FUNCTION: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. {ECO:0000255|HAMAP-Rule:MF_00997}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Metal binding (3); Repeat (4); Signal peptide (1) |
Keywords | Hydrolase;Metal-binding;Metalloprotease;Periplasm;Protease;Reference proteome;Repeat;Signal;TPR repeat;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00997}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255|HAMAP-Rule:MF_00997 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 54,104 |
Kinetics | |
Metal Binding | METAL 133; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00997; METAL 137; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00997; METAL 198; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00997 |
Rhea ID | |
Cross Reference Brenda |