THER_BACTH
ID THER_BACTH Reviewed; 548 AA.
AC P00800; Q45779;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Thermolysin;
DE EC=3.4.24.27;
DE AltName: Full=Thermostable neutral proteinase;
DE Flags: Precursor;
GN Name=npr;
OS Bacillus thermoproteolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1427;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rokko;
RX PubMed=8002967; DOI=10.1042/bj3000599;
RA O'Donohue M.J., Roques B.P., Beaumont A.;
RT "Cloning and expression in Bacillus subtilis of the npr gene from Bacillus
RT thermoproteolyticus Rokko coding for the thermostable metalloprotease
RT thermolysin.";
RL Biochem. J. 300:599-603(1994).
RN [2]
RP PROTEIN SEQUENCE OF 233-548.
RA Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.;
RT "Amino-acid sequence of thermolysin.";
RL Nature New Biol. 238:35-37(1972).
RN [3]
RP PROTEIN SEQUENCE OF 233-268; 352-400 AND 438-477.
RX PubMed=5040648; DOI=10.1021/bi00763a007;
RA Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.;
RT "Amino acid sequence of thermolysin. Isolation and characterization of the
RT fragments obtained by cleavage with cyanogen bromide.";
RL Biochemistry 11:2427-2435(1972).
RN [4]
RP ACTIVE SITE.
RX PubMed=4808703; DOI=10.1021/bi00698a030;
RA Burstein Y., Walsh K.A., Neurath H.;
RT "Evidence of an essential histidine residue in thermolysin.";
RL Biochemistry 13:205-210(1974).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=7175940; DOI=10.1016/0022-2836(82)90319-9;
RA Holmes M.A., Matthews B.W.;
RT "Structure of thermolysin refined at 1.6-A resolution.";
RL J. Mol. Biol. 160:623-639(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=4214815; DOI=10.1016/s0021-9258(19)42067-x;
RA Matthews B.W., Weaver L.H., Kester W.R.;
RT "The conformation of thermolysin.";
RL J. Biol. Chem. 249:8030-8044(1974).
RN [7]
RP STRUCTURE BY NMR OF 487-548.
RX PubMed=7993910; DOI=10.1021/bi00253a023;
RA Rico M., Jimenez M.A., Gonzalez C., de Filippis V., Fontana A.;
RT "NMR solution structure of the C-terminal fragment 255-316 of thermolysin:
RT a dimer formed by subunits having the native structure.";
RL Biochemistry 33:14834-14847(1994).
RN [8]
RP STRUCTURE BY NMR OF 437-548.
RX PubMed=9305992; DOI=10.1021/bi971060t;
RA Conejero-Lara F., Gonzalez C., Jimenez M.A., Padmanabhan S., Mateo P.L.,
RA Rico M.;
RT "NMR solution structure of the 205-316 C-terminal fragment of thermolysin.
RT An example of dimerization coupled to partial unfolding.";
RL Biochemistry 36:11975-11983(1997).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.; EC=3.4.24.27;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 4 Ca(2+) ions per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; X76986; CAA54291.1; -; Genomic_DNA.
DR PIR; I40579; HYBST.
DR PDB; 1FJ3; X-ray; 2.00 A; A=233-548.
DR PDB; 1FJO; X-ray; 2.00 A; A=233-548.
DR PDB; 1FJQ; X-ray; 1.70 A; A=233-548.
DR PDB; 1FJT; X-ray; 2.20 A; A=233-548.
DR PDB; 1FJU; X-ray; 2.00 A; A=233-548.
DR PDB; 1FJV; X-ray; 2.00 A; A=233-548.
DR PDB; 1FJW; X-ray; 1.90 A; A=233-548.
DR PDB; 1GXW; X-ray; 2.18 A; A=233-548.
DR PDB; 1HYT; X-ray; 1.70 A; A=233-548.
DR PDB; 1KEI; X-ray; 1.60 A; A=233-548.
DR PDB; 1KJO; X-ray; 1.60 A; A=233-548.
DR PDB; 1KJP; X-ray; 1.60 A; A=233-548.
DR PDB; 1KKK; X-ray; 1.60 A; A=233-548.
DR PDB; 1KL6; X-ray; 1.80 A; A=233-548.
DR PDB; 1KR6; X-ray; 1.80 A; A=233-548.
DR PDB; 1KRO; X-ray; 1.70 A; A=233-548.
DR PDB; 1KS7; X-ray; 1.70 A; A=233-548.
DR PDB; 1KTO; X-ray; 1.90 A; A=233-548.
DR PDB; 1L3F; X-ray; 2.30 A; E=233-548.
DR PDB; 1LNA; X-ray; 1.90 A; E=233-548.
DR PDB; 1LNB; X-ray; 1.80 A; E=233-548.
DR PDB; 1LNC; X-ray; 1.80 A; E=233-548.
DR PDB; 1LND; X-ray; 1.70 A; E=233-548.
DR PDB; 1LNE; X-ray; 1.70 A; E=233-548.
DR PDB; 1LNF; X-ray; 1.70 A; E=233-548.
DR PDB; 1OS0; X-ray; 2.10 A; A=233-548.
DR PDB; 1PE5; X-ray; 1.70 A; A=233-548.
DR PDB; 1PE7; X-ray; 1.82 A; A=233-548.
DR PDB; 1PE8; X-ray; 1.80 A; A=233-548.
DR PDB; 1QF0; X-ray; 2.20 A; A=233-548.
DR PDB; 1QF1; X-ray; 2.00 A; A=233-548.
DR PDB; 1QF2; X-ray; 2.06 A; A=233-548.
DR PDB; 1THL; X-ray; 1.70 A; A=233-548.
DR PDB; 1TLI; X-ray; 2.05 A; A=233-548.
DR PDB; 1TLP; X-ray; 2.30 A; E=233-548.
DR PDB; 1TLX; X-ray; 2.10 A; A=233-548.
DR PDB; 1TMN; X-ray; 1.90 A; E=233-548.
DR PDB; 1TRL; NMR; -; A/B=487-548.
DR PDB; 1Y3G; X-ray; 2.10 A; E=233-548.
DR PDB; 1Z9G; X-ray; 1.70 A; E=233-548.
DR PDB; 1ZDP; X-ray; 1.70 A; E=233-548.
DR PDB; 2A7G; X-ray; 1.85 A; E=233-548.
DR PDB; 2G4Z; X-ray; 1.98 A; A=233-548.
DR PDB; 2TLI; X-ray; 1.95 A; A=233-548.
DR PDB; 2TLX; X-ray; 1.65 A; A=233-548.
DR PDB; 2TMN; X-ray; 1.60 A; E=233-548.
DR PDB; 2WHZ; X-ray; 1.75 A; A=233-548.
DR PDB; 2WI0; X-ray; 1.95 A; A=233-548.
DR PDB; 3DNZ; X-ray; 1.20 A; A=233-548.
DR PDB; 3DO0; X-ray; 1.36 A; A=233-548.
DR PDB; 3DO1; X-ray; 1.33 A; A=233-548.
DR PDB; 3DO2; X-ray; 1.22 A; A=233-548.
DR PDB; 3EIM; X-ray; 1.88 A; A=233-548.
DR PDB; 3F28; X-ray; 1.68 A; A=233-548.
DR PDB; 3F2P; X-ray; 1.95 A; A=233-548.
DR PDB; 3FB0; X-ray; 1.60 A; A=233-548.
DR PDB; 3FBO; X-ray; 1.92 A; A=233-548.
DR PDB; 3FCQ; X-ray; 1.75 A; A=233-548.
DR PDB; 3FGD; X-ray; 1.33 A; A=233-548.
DR PDB; 3FLF; X-ray; 1.97 A; A=233-548.
DR PDB; 3FOR; X-ray; 1.93 A; A=233-548.
DR PDB; 3FV4; X-ray; 1.56 A; A=233-548.
DR PDB; 3FVP; X-ray; 1.41 A; A=233-548.
DR PDB; 3FXP; X-ray; 2.05 A; A=233-548.
DR PDB; 3FXS; X-ray; 1.55 A; A=233-548.
DR PDB; 3LS7; X-ray; 1.98 A; A=233-548.
DR PDB; 3MS3; X-ray; 1.54 A; A=233-548.
DR PDB; 3MSA; X-ray; 1.66 A; A=233-548.
DR PDB; 3MSF; X-ray; 2.09 A; A=233-548.
DR PDB; 3MSN; X-ray; 1.97 A; A=233-548.
DR PDB; 3N21; X-ray; 1.87 A; A=233-548.
DR PDB; 3NN7; X-ray; 2.05 A; A=233-548.
DR PDB; 3P7P; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7Q; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7R; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7S; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7T; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7U; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7V; X-ray; 2.20 A; E=233-548.
DR PDB; 3P7W; X-ray; 2.20 A; E=233-548.
DR PDB; 3QGO; X-ray; 1.45 A; A=233-548.
DR PDB; 3QH1; X-ray; 1.55 A; A=233-548.
DR PDB; 3QH5; X-ray; 1.50 A; A=233-548.
DR PDB; 3SSB; X-ray; 1.80 A; A/B=233-548.
DR PDB; 3T2H; X-ray; 1.95 A; E=233-548.
DR PDB; 3T2I; X-ray; 2.10 A; E=233-548.
DR PDB; 3T2J; X-ray; 2.00 A; E=233-548.
DR PDB; 3T73; X-ray; 1.60 A; A=233-548.
DR PDB; 3T74; X-ray; 1.28 A; A=233-548.
DR PDB; 3T87; X-ray; 1.28 A; A=233-548.
DR PDB; 3T8C; X-ray; 1.66 A; A=233-548.
DR PDB; 3T8D; X-ray; 1.41 A; A=233-548.
DR PDB; 3T8F; X-ray; 1.44 A; A=233-548.
DR PDB; 3T8G; X-ray; 1.50 A; A=233-548.
DR PDB; 3T8H; X-ray; 1.45 A; A=233-548.
DR PDB; 3TLI; X-ray; 1.95 A; A=233-548.
DR PDB; 3TMN; X-ray; 1.70 A; E=233-548.
DR PDB; 3ZI6; X-ray; 2.00 A; A=233-548.
DR PDB; 4D91; X-ray; 1.90 A; A=233-548.
DR PDB; 4D9W; X-ray; 1.38 A; A=233-548.
DR PDB; 4H57; X-ray; 1.56 A; A=233-548.
DR PDB; 4MTW; X-ray; 1.32 A; E=233-548.
DR PDB; 4MWP; X-ray; 1.23 A; E=233-548.
DR PDB; 4MXJ; X-ray; 1.35 A; E=233-548.
DR PDB; 4MZN; X-ray; 1.17 A; E=233-548.
DR PDB; 4N4E; X-ray; 1.13 A; E=233-548.
DR PDB; 4N5P; X-ray; 1.25 A; E=233-548.
DR PDB; 4N66; X-ray; 1.44 A; E=233-548.
DR PDB; 4OI5; X-ray; 1.30 A; E=233-548.
DR PDB; 4OW3; X-ray; 2.10 A; A=233-548.
DR PDB; 4TLI; X-ray; 1.95 A; A=233-548.
DR PDB; 4TLN; X-ray; 2.30 A; A=233-548.
DR PDB; 4TMN; X-ray; 1.70 A; E=233-548.
DR PDB; 4TNL; X-ray; 1.80 A; A=233-548.
DR PDB; 5A3Y; X-ray; 1.27 A; A=1-548.
DR PDB; 5DPE; X-ray; 1.34 A; E=233-548.
DR PDB; 5DPF; X-ray; 1.47 A; E=233-548.
DR PDB; 5FSJ; X-ray; 1.20 A; A=233-548.
DR PDB; 5FSP; X-ray; 1.70 A; A=233-548.
DR PDB; 5FSS; X-ray; 1.50 A; A=233-548.
DR PDB; 5FXN; X-ray; 1.45 A; A=234-548.
DR PDB; 5JS3; X-ray; 1.16 A; E=233-548.
DR PDB; 5JSS; X-ray; 1.19 A; E=233-548.
DR PDB; 5JT9; X-ray; 1.26 A; E=233-548.
DR PDB; 5JVI; X-ray; 1.12 A; E=233-548.
DR PDB; 5JXN; X-ray; 1.38 A; E=233-548.
DR PDB; 5K7T; EM; 2.50 A; A=233-548.
DR PDB; 5L3U; X-ray; 1.23 A; E=233-548.
DR PDB; 5L41; X-ray; 1.25 A; E=233-548.
DR PDB; 5L8P; X-ray; 1.29 A; E=233-548.
DR PDB; 5LIF; X-ray; 1.31 A; E=233-548.
DR PDB; 5LVD; X-ray; 1.25 A; E=233-548.
DR PDB; 5LWD; X-ray; 1.23 A; E=233-548.
DR PDB; 5M5F; X-ray; 1.33 A; E=233-548.
DR PDB; 5M69; X-ray; 1.44 A; E=233-548.
DR PDB; 5M9W; X-ray; 1.21 A; A=233-548.
DR PDB; 5MA7; X-ray; 1.30 A; E=233-548.
DR PDB; 5MNR; X-ray; 1.25 A; E=233-548.
DR PDB; 5N2T; X-ray; 1.38 A; E=233-548.
DR PDB; 5N2X; X-ray; 1.21 A; E=233-548.
DR PDB; 5N2Z; X-ray; 1.37 A; E=233-548.
DR PDB; 5N31; X-ray; 1.37 A; E=233-548.
DR PDB; 5N34; X-ray; 1.22 A; E=233-548.
DR PDB; 5N3V; X-ray; 1.12 A; E=233-548.
DR PDB; 5N3Y; X-ray; 1.34 A; E=233-548.
DR PDB; 5O8N; X-ray; 1.90 A; A=233-548.
DR PDB; 5ONR; X-ray; 1.39 A; A=233-548.
DR PDB; 5T9I; X-ray; 2.09 A; A=233-548.
DR PDB; 5T9K; X-ray; 2.10 A; A=233-548.
DR PDB; 5T9Q; X-ray; 2.10 A; A=233-548.
DR PDB; 5TAC; X-ray; 2.04 A; A=233-548.
DR PDB; 5TAD; X-ray; 2.09 A; A=233-548.
DR PDB; 5TAE; X-ray; 2.30 A; A=233-548.
DR PDB; 5TAI; X-ray; 2.30 A; A=233-548.
DR PDB; 5TAJ; X-ray; 2.03 A; A=233-548.
DR PDB; 5TAK; X-ray; 2.00 A; A=233-548.
DR PDB; 5TLI; X-ray; 2.10 A; A=233-548.
DR PDB; 5TLN; X-ray; 2.30 A; A=233-548.
DR PDB; 5TMN; X-ray; 1.60 A; E=233-548.
DR PDB; 5UN3; X-ray; 1.60 A; A=233-548.
DR PDB; 5UU7; X-ray; 1.60 A; A=233-548.
DR PDB; 5UU8; X-ray; 2.50 A; A=233-548.
DR PDB; 5UU9; X-ray; 1.60 A; A=233-548.
DR PDB; 5UUA; X-ray; 1.60 A; A=233-548.
DR PDB; 5UUB; X-ray; 1.60 A; A=233-548.
DR PDB; 5UUC; X-ray; 1.60 A; A=233-548.
DR PDB; 5UUD; X-ray; 1.60 A; A=233-548.
DR PDB; 5UUE; X-ray; 1.60 A; A=233-548.
DR PDB; 6D5N; X-ray; 2.00 A; A=233-548.
DR PDB; 6D5O; X-ray; 2.00 A; A=233-548.
DR PDB; 6D5P; X-ray; 3.00 A; A=233-548.
DR PDB; 6D5Q; X-ray; 2.00 A; A=233-548.
DR PDB; 6D5R; X-ray; 2.00 A; A=233-548.
DR PDB; 6D5S; X-ray; 2.00 A; A=233-548.
DR PDB; 6D5T; X-ray; 2.00 A; A=233-548.
DR PDB; 6D5U; X-ray; 2.00 A; A=233-548.
DR PDB; 6FJ2; X-ray; 1.43 A; A=233-548.
DR PDB; 6IG7; X-ray; 1.80 A; A=233-548.
DR PDB; 6LZN; X-ray; 1.50 A; A=233-548.
DR PDB; 6LZO; X-ray; 1.80 A; A=233-548.
DR PDB; 6N4W; X-ray; 1.40 A; A=233-548.
DR PDB; 6N4Z; X-ray; 1.40 A; A=233-548.
DR PDB; 6QAR; X-ray; 1.85 A; A=233-548.
DR PDB; 6QF2; X-ray; 1.73 A; A=233-548.
DR PDB; 6QF3; X-ray; 1.52 A; A=233-548.
DR PDB; 6SB9; X-ray; 1.30 A; E=233-548.
DR PDB; 6SBK; X-ray; 1.48 A; E=233-548.
DR PDB; 6SC0; X-ray; 1.53 A; E=233-548.
DR PDB; 6SC1; X-ray; 1.56 A; E=233-548.
DR PDB; 6SC3; X-ray; 1.82 A; E=233-548.
DR PDB; 6SCK; X-ray; 1.41 A; E=233-548.
DR PDB; 6SCU; X-ray; 1.42 A; E=233-548.
DR PDB; 6SEL; X-ray; 2.20 A; A=233-548.
DR PDB; 6TLI; X-ray; 2.10 A; A=233-548.
DR PDB; 6TMN; X-ray; 1.60 A; E=233-548.
DR PDB; 6ZHJ; EM; 3.26 A; A=233-548.
DR PDB; 7AKN; X-ray; 2.46 A; A=233-548.
DR PDB; 7TLI; X-ray; 1.95 A; A=233-548.
DR PDB; 7TLN; X-ray; 2.30 A; A=233-548.
DR PDB; 8TLI; X-ray; 2.20 A; A=233-548.
DR PDB; 8TLN; X-ray; 1.60 A; E=233-548.
DR PDBsum; 1FJ3; -.
DR PDBsum; 1FJO; -.
DR PDBsum; 1FJQ; -.
DR PDBsum; 1FJT; -.
DR PDBsum; 1FJU; -.
DR PDBsum; 1FJV; -.
DR PDBsum; 1FJW; -.
DR PDBsum; 1GXW; -.
DR PDBsum; 1HYT; -.
DR PDBsum; 1KEI; -.
DR PDBsum; 1KJO; -.
DR PDBsum; 1KJP; -.
DR PDBsum; 1KKK; -.
DR PDBsum; 1KL6; -.
DR PDBsum; 1KR6; -.
DR PDBsum; 1KRO; -.
DR PDBsum; 1KS7; -.
DR PDBsum; 1KTO; -.
DR PDBsum; 1L3F; -.
DR PDBsum; 1LNA; -.
DR PDBsum; 1LNB; -.
DR PDBsum; 1LNC; -.
DR PDBsum; 1LND; -.
DR PDBsum; 1LNE; -.
DR PDBsum; 1LNF; -.
DR PDBsum; 1OS0; -.
DR PDBsum; 1PE5; -.
DR PDBsum; 1PE7; -.
DR PDBsum; 1PE8; -.
DR PDBsum; 1QF0; -.
DR PDBsum; 1QF1; -.
DR PDBsum; 1QF2; -.
DR PDBsum; 1THL; -.
DR PDBsum; 1TLI; -.
DR PDBsum; 1TLP; -.
DR PDBsum; 1TLX; -.
DR PDBsum; 1TMN; -.
DR PDBsum; 1TRL; -.
DR PDBsum; 1Y3G; -.
DR PDBsum; 1Z9G; -.
DR PDBsum; 1ZDP; -.
DR PDBsum; 2A7G; -.
DR PDBsum; 2G4Z; -.
DR PDBsum; 2TLI; -.
DR PDBsum; 2TLX; -.
DR PDBsum; 2TMN; -.
DR PDBsum; 2WHZ; -.
DR PDBsum; 2WI0; -.
DR PDBsum; 3DNZ; -.
DR PDBsum; 3DO0; -.
DR PDBsum; 3DO1; -.
DR PDBsum; 3DO2; -.
DR PDBsum; 3EIM; -.
DR PDBsum; 3F28; -.
DR PDBsum; 3F2P; -.
DR PDBsum; 3FB0; -.
DR PDBsum; 3FBO; -.
DR PDBsum; 3FCQ; -.
DR PDBsum; 3FGD; -.
DR PDBsum; 3FLF; -.
DR PDBsum; 3FOR; -.
DR PDBsum; 3FV4; -.
DR PDBsum; 3FVP; -.
DR PDBsum; 3FXP; -.
DR PDBsum; 3FXS; -.
DR PDBsum; 3LS7; -.
DR PDBsum; 3MS3; -.
DR PDBsum; 3MSA; -.
DR PDBsum; 3MSF; -.
DR PDBsum; 3MSN; -.
DR PDBsum; 3N21; -.
DR PDBsum; 3NN7; -.
DR PDBsum; 3P7P; -.
DR PDBsum; 3P7Q; -.
DR PDBsum; 3P7R; -.
DR PDBsum; 3P7S; -.
DR PDBsum; 3P7T; -.
DR PDBsum; 3P7U; -.
DR PDBsum; 3P7V; -.
DR PDBsum; 3P7W; -.
DR PDBsum; 3QGO; -.
DR PDBsum; 3QH1; -.
DR PDBsum; 3QH5; -.
DR PDBsum; 3SSB; -.
DR PDBsum; 3T2H; -.
DR PDBsum; 3T2I; -.
DR PDBsum; 3T2J; -.
DR PDBsum; 3T73; -.
DR PDBsum; 3T74; -.
DR PDBsum; 3T87; -.
DR PDBsum; 3T8C; -.
DR PDBsum; 3T8D; -.
DR PDBsum; 3T8F; -.
DR PDBsum; 3T8G; -.
DR PDBsum; 3T8H; -.
DR PDBsum; 3TLI; -.
DR PDBsum; 3TMN; -.
DR PDBsum; 3ZI6; -.
DR PDBsum; 4D91; -.
DR PDBsum; 4D9W; -.
DR PDBsum; 4H57; -.
DR PDBsum; 4MTW; -.
DR PDBsum; 4MWP; -.
DR PDBsum; 4MXJ; -.
DR PDBsum; 4MZN; -.
DR PDBsum; 4N4E; -.
DR PDBsum; 4N5P; -.
DR PDBsum; 4N66; -.
DR PDBsum; 4OI5; -.
DR PDBsum; 4OW3; -.
DR PDBsum; 4TLI; -.
DR PDBsum; 4TLN; -.
DR PDBsum; 4TMN; -.
DR PDBsum; 4TNL; -.
DR PDBsum; 5A3Y; -.
DR PDBsum; 5DPE; -.
DR PDBsum; 5DPF; -.
DR PDBsum; 5FSJ; -.
DR PDBsum; 5FSP; -.
DR PDBsum; 5FSS; -.
DR PDBsum; 5FXN; -.
DR PDBsum; 5JS3; -.
DR PDBsum; 5JSS; -.
DR PDBsum; 5JT9; -.
DR PDBsum; 5JVI; -.
DR PDBsum; 5JXN; -.
DR PDBsum; 5K7T; -.
DR PDBsum; 5L3U; -.
DR PDBsum; 5L41; -.
DR PDBsum; 5L8P; -.
DR PDBsum; 5LIF; -.
DR PDBsum; 5LVD; -.
DR PDBsum; 5LWD; -.
DR PDBsum; 5M5F; -.
DR PDBsum; 5M69; -.
DR PDBsum; 5M9W; -.
DR PDBsum; 5MA7; -.
DR PDBsum; 5MNR; -.
DR PDBsum; 5N2T; -.
DR PDBsum; 5N2X; -.
DR PDBsum; 5N2Z; -.
DR PDBsum; 5N31; -.
DR PDBsum; 5N34; -.
DR PDBsum; 5N3V; -.
DR PDBsum; 5N3Y; -.
DR PDBsum; 5O8N; -.
DR PDBsum; 5ONR; -.
DR PDBsum; 5T9I; -.
DR PDBsum; 5T9K; -.
DR PDBsum; 5T9Q; -.
DR PDBsum; 5TAC; -.
DR PDBsum; 5TAD; -.
DR PDBsum; 5TAE; -.
DR PDBsum; 5TAI; -.
DR PDBsum; 5TAJ; -.
DR PDBsum; 5TAK; -.
DR PDBsum; 5TLI; -.
DR PDBsum; 5TLN; -.
DR PDBsum; 5TMN; -.
DR PDBsum; 5UN3; -.
DR PDBsum; 5UU7; -.
DR PDBsum; 5UU8; -.
DR PDBsum; 5UU9; -.
DR PDBsum; 5UUA; -.
DR PDBsum; 5UUB; -.
DR PDBsum; 5UUC; -.
DR PDBsum; 5UUD; -.
DR PDBsum; 5UUE; -.
DR PDBsum; 6D5N; -.
DR PDBsum; 6D5O; -.
DR PDBsum; 6D5P; -.
DR PDBsum; 6D5Q; -.
DR PDBsum; 6D5R; -.
DR PDBsum; 6D5S; -.
DR PDBsum; 6D5T; -.
DR PDBsum; 6D5U; -.
DR PDBsum; 6FJ2; -.
DR PDBsum; 6IG7; -.
DR PDBsum; 6LZN; -.
DR PDBsum; 6LZO; -.
DR PDBsum; 6N4W; -.
DR PDBsum; 6N4Z; -.
DR PDBsum; 6QAR; -.
DR PDBsum; 6QF2; -.
DR PDBsum; 6QF3; -.
DR PDBsum; 6SB9; -.
DR PDBsum; 6SBK; -.
DR PDBsum; 6SC0; -.
DR PDBsum; 6SC1; -.
DR PDBsum; 6SC3; -.
DR PDBsum; 6SCK; -.
DR PDBsum; 6SCU; -.
DR PDBsum; 6SEL; -.
DR PDBsum; 6TLI; -.
DR PDBsum; 6TMN; -.
DR PDBsum; 6ZHJ; -.
DR PDBsum; 7AKN; -.
DR PDBsum; 7TLI; -.
DR PDBsum; 7TLN; -.
DR PDBsum; 8TLI; -.
DR PDBsum; 8TLN; -.
DR AlphaFoldDB; P00800; -.
DR BMRB; P00800; -.
DR SMR; P00800; -.
DR BindingDB; P00800; -.
DR ChEMBL; CHEMBL3392; -.
DR DrugBank; DB07673; (2S)-2-Methyl-3-phenylpropanoic acid.
DR DrugBank; DB07487; (6-METHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL)METHYLPHOSPHINATE.
DR DrugBank; DB07103; 2-(4-METHYLPHENOXY)ETHYLPHOSPHINATE.
DR DrugBank; DB07989; 2-(ACETYL-HYDROXY-AMINO)-4-METHYL-PENTANOIC ACID METHYL ESTER.
DR DrugBank; DB01935; 3-{[(1r)-1-Benzyl-2-Sulfanylethyl]Amino}-3-Oxopropanoic Acid.
DR DrugBank; DB02597; [2(R,S)-2-Sulfanylheptanoyl]-Phe-Ala.
DR DrugBank; DB07434; HONH-BENZYLMALONYL-L-ALANYLGLYCINE-P-NITROANILIDE.
DR DrugBank; DB07506; L-BENZYLSUCCINIC ACID.
DR DrugBank; DB03255; Phenol.
DR DrugBank; DB06819; Phenylbutyric acid.
DR DrugBank; DB02669; RB106.
DR DrugCentral; P00800; -.
DR MEROPS; M04.001; -.
DR KEGG; ag:CAA54291; -.
DR BRENDA; 3.4.24.27; 708.
DR SABIO-RK; P00800; -.
DR EvolutionaryTrace; P00800; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR DisProt; DP02501; -.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT PROPEP 29..232
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:5040648, ECO:0000269|Ref.2"
FT /id="PRO_0000028592"
FT CHAIN 233..548
FT /note="Thermolysin"
FT /id="PRO_0000028593"
FT ACT_SITE 375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:4808703"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:4808703"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT CONFLICT 269
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="I -> M (in Ref. 1; CAA54291)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="E -> K (in Ref. 1; CAA54291)"
FT /evidence="ECO:0000305"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 249..264
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6ZHJ"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 300..320
FT /evidence="ECO:0007829|PDB:5JVI"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 391..412
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:5JVI"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:6SBK"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:5JVI"
FT TURN 462..465
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5JVI"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 492..505
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 513..528
FT /evidence="ECO:0007829|PDB:5JVI"
FT HELIX 533..544
FT /evidence="ECO:0007829|PDB:5JVI"
SQ SEQUENCE 548 AA; 60104 MW; 1D6ED3A545F045C8 CRC64;
MKMKMKLASF GLAAGLAAQV FLPYNALAST EHVTWNQQFQ TPQFISGDLL KVNGTSPEEL
VYQYVEKNEN KFKFHENAKD TLQLKEKKND NLGFTFMRFQ QTYKGIPVFG AVVTSHVKDG
TLTALSGTLI PNLDTKGSLK SGKKLSEKQA RDIAEKDLVA NVTKEVPEYE QGKDTEFVVY
VNGDEASLAY VVNLNFLTPE PGNWLYIIDA VDGKILNKFN QLDAAKPGDV KSITGTSTVG
VGRGVLGDQK NINTTYSTYY YLQDNTRGNG IFTYDAKYRT TLPGSLWADA DNQFFASYDA
PAVDAHYYAG VTYDYYKNVH NRLSYDGNNA AIRSSVHYSQ GYNNAFWNGS QMVYGDGDGQ
TFIPLSGGID VVAHELTHAV TDYTAGLIYQ NESGAINEAI SDIFGTLVEF YANKNPDWEI
GEDVYTPGIS GDSLRSMSDP AKYGDPDHYS KRYTGTQDNG GVHINSGIIN KAAYLISQGG
THYGVSVVGI GRDKLGKIFY RALTQYLTPT SNFSQLRAAA VQSATDLYGS TSQEVASVKQ
AFDAVGVK
