| IED ID | IndEnz0002012877 |
| Enzyme Type ID | protease012877 |
| Protein Name |
Thermolysin EC 3.4.24.27 Thermostable neutral proteinase |
| Gene Name | npr |
| Organism | Bacillus thermoproteolyticus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus thermoproteolyticus |
| Enzyme Sequence | MKMKMKLASFGLAAGLAAQVFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTSHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK |
| Enzyme Length | 548 |
| Uniprot Accession Number | P00800 |
| Absorption | |
| Active Site | ACT_SITE 375; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703"; ACT_SITE 463; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.; EC=3.4.24.27; |
| DNA Binding | |
| EC Number | 3.4.24.27 |
| Enzyme Function | FUNCTION: Extracellular zinc metalloprotease. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable.; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (1); Helix (12); Metal binding (19); Propeptide (1); Sequence conflict (4); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000250 |
| Structure 3D | NMR spectroscopy (1); Electron microscopy (2); X-ray crystallography (198) |
| Cross Reference PDB | 1FJ3; 1FJO; 1FJQ; 1FJT; 1FJU; 1FJV; 1FJW; 1GXW; 1HYT; 1KEI; 1KJO; 1KJP; 1KKK; 1KL6; 1KR6; 1KRO; 1KS7; 1KTO; 1L3F; 1LNA; 1LNB; 1LNC; 1LND; 1LNE; 1LNF; 1OS0; 1PE5; 1PE7; 1PE8; 1QF0; 1QF1; 1QF2; 1THL; 1TLI; 1TLP; 1TLX; 1TMN; 1TRL; 1Y3G; 1Z9G; 1ZDP; 2A7G; 2G4Z; 2TLI; 2TLX; 2TMN; 2WHZ; 2WI0; 3DNZ; 3DO0; 3DO1; 3DO2; 3EIM; 3F28; 3F2P; 3FB0; 3FBO; 3FCQ; 3FGD; 3FLF; 3FOR; 3FV4; 3FVP; 3FXP; 3FXS; 3LS7; 3MS3; 3MSA; 3MSF; 3MSN; 3N21; 3NN7; 3P7P; 3P7Q; 3P7R; 3P7S; 3P7T; 3P7U; 3P7V; 3P7W; 3QGO; 3QH1; 3QH5; 3SSB; 3T2H; 3T2I; 3T2J; 3T73; 3T74; 3T87; 3T8C; 3T8D; 3T8F; 3T8G; 3T8H; 3TLI; 3TMN; 3ZI6; 4D91; 4D9W; 4H57; 4MTW; 4MWP; 4MXJ; 4MZN; 4N4E; 4N5P; 4N66; 4OI5; 4OW3; 4TLI; 4TLN; 4TMN; 4TNL; 5A3Y; 5DPE; 5DPF; 5FSJ; 5FSP; 5FSS; 5FXN; 5JS3; 5JSS; 5JT9; 5JVI; 5JXN; 5K7T; 5L3U; 5L41; 5L8P; 5LIF; 5LVD; 5LWD; 5M5F; 5M69; 5M9W; 5MA7; 5MNR; 5N2T; 5N2X; 5N2Z; 5N31; 5N34; 5N3V; 5N3Y; 5O8N; 5ONR; 5T9I; 5T9K; 5T9Q; 5TAC; 5TAD; 5TAE; 5TAI; 5TAJ; 5TAK; 5TLI; 5TLN; 5TMN; 5UN3; 5UU7; 5UU8; 5UU9; 5UUA; 5UUB; 5UUC; 5UUD; 5UUE; 6D5N; 6D5O; 6D5P; 6D5Q; 6D5R; 6D5S; 6D5T; 6D5U; 6FJ2; 6IG7; 6LZN; 6LZO; 6N4W; 6N4Z; 6QAR; 6QF2; 6QF3; 6SB9; 6SBK; 6SC0; 6SC1; 6SC3; 6SCK; 6SCU; 6SEL; 6TLI; 6TMN; 6ZHJ; 7AKN; 7TLI; 7TLN; 8TLI; 8TLN; |
| Mapped Pubmed ID | 10504225; 10651278; 11287678; 12037302; 12454500; 12832763; 1445869; 16131760; 16342943; 17327674; 18663849; 20124702; 20394106; 20600625; 21915964; 22194335; 22213702; 22505256; 22733601; 23090408; 23283700; 23656378; 23793153; 24623396; 24633409; 24944748; 25006873; 26376645; 26527148; 2719912; 27487827; 27933956; 27959500; 28192420; 28590130; 28696673; 29124258; 29979188; 30198901; 30403288; 30792457; 31316815; 31636524; 33310458; 33404527; 3343246; 3442675; 3709536; 3810156; 6395881; 6830761; 7317361; 8034637; 8286362; 8535232; 8632427; 8691458; 9562615; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,104 |
| Kinetics | |
| Metal Binding | METAL 289; /note=Calcium 1; METAL 291; /note=Calcium 1; METAL 293; /note=Calcium 1; via carbonyl oxygen; METAL 370; /note=Calcium 2; METAL 374; /note=Zinc; catalytic; METAL 378; /note=Zinc; catalytic; METAL 398; /note=Zinc; catalytic; METAL 409; /note=Calcium 2; METAL 409; /note=Calcium 3; METAL 415; /note=Calcium 3; via carbonyl oxygen; METAL 417; /note=Calcium 2; METAL 417; /note=Calcium 3; METAL 419; /note=Calcium 2; via carbonyl oxygen; METAL 422; /note=Calcium 2; METAL 422; /note=Calcium 3; METAL 425; /note=Calcium 4; via carbonyl oxygen; METAL 426; /note=Calcium 4; METAL 429; /note=Calcium 4; via carbonyl oxygen; METAL 432; /note=Calcium 4 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.27; |