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   04-NOV-2026, entry version 180.
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; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   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.
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.
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   PDB; 8ZM4; X-ray; 1.40 A; A=233-548.
DR   PDB; 8ZM5; X-ray; 1.40 A; A=233-548.
DR   PDB; 8ZM6; X-ray; 1.40 A; A=233-548.
DR   PDB; 9F56; X-ray; 2.10 A; A=233-548.
DR   AlphaFoldDB; P00800; -.
DR   BMRB; P00800; -.
DR   EMDB; EMD-8222; -.
DR   MDposit; P00800; -.
DR   MDRepo; 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; 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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd09597; M4_TLP; 1.
DR   DisProt; DP02501; -.
DR   FunFam; 1.10.390.10:FF:000012; Thermolysin; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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   InterPro; IPR050728; Zinc_Metalloprotease_M4.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF3; NEUTRAL PROTEASE B; 1.
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   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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:8ZM6"
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..501
FT                   /evidence="ECO:0007829|PDB:5JVI"
FT   HELIX           502..506
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
//