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UniProtKB/Swiss-Prot entry P00800

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name THER_BACTH
Primary accession number P00800
Secondary accession number Q45779
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on April 18, 2006 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 89)
Name and origin of the protein
Protein name Thermolysin [Precursor]
Synonyms EC 3.4.24.27
Thermostable neutral proteinase
Gene name
Name: npr
From
Bacillus thermoproteolyticus [TaxID: 1427] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Rokko;
PubMed=8002967 [NCBI, ExPASy, EBI, Israel, Japan]
O'Donohue M.J., Roques B.P., Beaumont A.;
"Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin.";
Biochem. J. 300:599-603(1994).
[2]
 PROTEIN SEQUENCE OF 233-548.
Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.;
"Amino-acid sequence of thermolysin.";
Nature New Biol. 238:35-37(1972).
[3]
 PROTEIN SEQUENCE OF 233-268; 352-400 AND 438-477.
DOI=10.1021/bi00763a007; PubMed=5040648 [NCBI, ExPASy, EBI, Israel, Japan]
Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.;
"Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide.";
Biochemistry 11:2427-2435(1972).
[4]
 ACTIVE SITE.
DOI=10.1021/bi00698a030; PubMed=4808703 [NCBI, ExPASy, EBI, Israel, Japan]
Burstein Y., Walsh K.A., Neurath H.;
"Evidence of an essential histidine residue in thermolysin.";
Biochemistry 13:205-210(1974).
[5]
 X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1016/0022-2836(82)90319-9; PubMed=7175940 [NCBI, ExPASy, EBI, Israel, Japan]
Holmes M.A., Matthews B.W.;
"Structure of thermolysin refined at 1.6-A resolution.";
J. Mol. Biol. 160:623-639(1982).
[6]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=4214815 [NCBI, ExPASy, EBI, Israel, Japan]
Matthews B.W., Weaver L.H., Kester W.R.;
"The conformation of thermolysin.";
J. Biol. Chem. 249:8030-8044(1974).
[7]
 STRUCTURE BY NMR OF 487-548.
DOI=10.1021/bi00253a023; PubMed=7993910 [NCBI, ExPASy, EBI, Israel, Japan]
Rico M., Jimenez M.A., Gonzalez C., de Filippis V., Fontana A.;
"NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure.";
Biochemistry 33:14834-14847(1994).
[8]
 STRUCTURE BY NMR OF 437-548.
DOI=10.1021/bi971060t; PubMed=9305992 [NCBI, ExPASy, EBI, Israel, Japan]
Conejero-Lara F., Gonzalez C., Jimenez M.A., Padmanabhan S., Mateo P.L., Rico M.;
"NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding.";
Biochemistry 36:11975-11983(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X76986; CAA54291.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I40579; HYBST.
3D structure databases
PDB
1FJ3; X-ray; 2.00 A; A=233-548.[ExPASy / RCSB / EBI]
1FJO; X-ray; 2.00 A; A=233-548.[ExPASy / RCSB / EBI]
1FJQ; X-ray; 1.70 A; A=233-548.[ExPASy / RCSB / EBI]
1FJT; X-ray; 2.20 A; A=233-548.[ExPASy / RCSB / EBI]
1FJU; X-ray; 2.00 A; A=233-548.[ExPASy / RCSB / EBI]
1FJV; X-ray; 2.00 A; A=233-548.[ExPASy / RCSB / EBI]
1FJW; X-ray; 1.90 A; A=233-548.[ExPASy / RCSB / EBI]
1GXW; X-ray; 2.18 A; A=233-548.[ExPASy / RCSB / EBI]
1HYT; X-ray; 1.70 A; A=233-548.[ExPASy / RCSB / EBI]
1KEI; X-ray; 1.60 A; A=233-548.[ExPASy / RCSB / EBI]
1KJO; X-ray; 1.60 A; A=233-548.[ExPASy / RCSB / EBI]
1KJP; X-ray; 1.60 A; A=233-548.[ExPASy / RCSB / EBI]
1KKK; X-ray; 1.60 A; A=233-548.[ExPASy / RCSB / EBI]
1KL6; X-ray; 1.80 A; A=233-548.[ExPASy / RCSB / EBI]
1KR6; X-ray; 1.80 A; A=233-548.[ExPASy / RCSB / EBI]
1KRO; X-ray; 1.70 A; A=233-548.[ExPASy / RCSB / EBI]
1KS7; X-ray; 1.70 A; A=233-548.[ExPASy / RCSB / EBI]
1KTO; X-ray; 1.90 A; A=233-548.[ExPASy / RCSB / EBI]
1L3F; X-ray; 2.30 A; E=233-548.[ExPASy / RCSB / EBI]
1LNA; X-ray; 1.90 A; E=233-548.[ExPASy / RCSB / EBI]
1LNB; X-ray; 1.80 A; E=233-548.[ExPASy / RCSB / EBI]
1LNC; X-ray; 1.80 A; E=233-548.[ExPASy / RCSB / EBI]
1LND; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
1LNE; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
1LNF; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
1OS0; X-ray; 2.10 A; A=233-548.[ExPASy / RCSB / EBI]
1PE5; X-ray; 1.70 A; A=233-548.[ExPASy / RCSB / EBI]
1PE7; X-ray; 1.82 A; A=233-548.[ExPASy / RCSB / EBI]
1PE8; X-ray; 1.80 A; A=233-548.[ExPASy / RCSB / EBI]
1QF0; X-ray; 2.20 A; A=233-548.[ExPASy / RCSB / EBI]
1QF1; X-ray; 2.00 A; A=233-548.[ExPASy / RCSB / EBI]
1QF2; X-ray; 2.06 A; A=233-548.[ExPASy / RCSB / EBI]
1THL; X-ray; 1.70 A; A=233-548.[ExPASy / RCSB / EBI]
1TLI; X-ray; 2.05 A; A=233-548.[ExPASy / RCSB / EBI]
1TLP; X-ray; 2.30 A; E=233-548.[ExPASy / RCSB / EBI]
1TLX; X-ray; 2.10 A; A=233-548.[ExPASy / RCSB / EBI]
1TMN; X-ray; 1.90 A; E=233-548.[ExPASy / RCSB / EBI]
1TRL; NMR; -; A/B=487-548.[ExPASy / RCSB / EBI]
1Y3G; X-ray; 2.10 A; E=233-548.[ExPASy / RCSB / EBI]
1Z9G; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
1ZDP; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
2A7G; X-ray; 1.85 A; E=233-548.[ExPASy / RCSB / EBI]
2G4Z; X-ray; 1.98 A; A=233-548.[ExPASy / RCSB / EBI]
2TLI; X-ray; 1.95 A; A=233-548.[ExPASy / RCSB / EBI]
2TLX; X-ray; 1.65 A; A=233-548.[ExPASy / RCSB / EBI]
2TMN; X-ray; 1.60 A; E=233-548.[ExPASy / RCSB / EBI]
3TLI; X-ray; 1.95 A; A=233-548.[ExPASy / RCSB / EBI]
3TMN; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
4TLI; X-ray; 1.95 A; A=233-548.[ExPASy / RCSB / EBI]
4TLN; X-ray; 2.30 A; A=233-548.[ExPASy / RCSB / EBI]
4TMN; X-ray; 1.70 A; E=233-548.[ExPASy / RCSB / EBI]
5TLI; X-ray; 2.10 A; A=233-548.[ExPASy / RCSB / EBI]
5TLN; X-ray; 2.30 A; A=233-548.[ExPASy / RCSB / EBI]
5TMN; X-ray; 1.60 A; E=233-548.[ExPASy / RCSB / EBI]
6TLI; X-ray; 2.10 A; A=233-548.[ExPASy / RCSB / EBI]
6TMN; X-ray; 1.60 A; E=233-548.[ExPASy / RCSB / EBI]
7TLI; X-ray; 1.95 A; A=233-548.[ExPASy / RCSB / EBI]
7TLN; X-ray; 2.30 A; A=233-548.[ExPASy / RCSB / EBI]
8TLI; X-ray; 2.20 A; A=233-548.[ExPASy / RCSB / EBI]
8TLN; X-ray; 1.60 A; E=233-548.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 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; -.
3TLI; -.
3TMN; -.
4TLI; -.
4TLN; -.
4TMN; -.
5TLI; -.
5TLN; -.
5TMN; -.
6TLI; -.
6TMN; -.
7TLI; -.
7TLN; -.
8TLI; -.
8TLN; -.
ModBase P00800.
Protein family/group databases
MEROPS M04.001; -.
Ontologies
GO
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005075; Pept_M4_propep_PepSY.
IPR006025; Pept_M_Zn_BS.
IPR013856; Peptidase_M4.
IPR001570; Peptidase_M4_C.
IPR011096; Propep_M4_M36.
Graphical view of domain structure.
Gene3D G3DSA:3.10.170.10; Peptidase_M4; 1.
G3DSA:1.10.390.10; Peptidase_M4/M36; 1.
Pfam PF07504; FTP; 1.
PF03413; PepSY; 1.
PF01447; Peptidase_M4; 1.
PF02868; Peptidase_M4_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00730; THERMOLYSIN.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS P00800.
ProtoNet P00800.
Other
LinkHub P00800; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     By similarity. 
PROPEP   29   232  204     Activation peptide. PRO_0000028592
CHAIN   233   548  316     Thermolysin. PRO_0000028593
ACT_SITE   375   375         
ACT_SITE   463   463        Proton donor. 
METAL   289   289        Calcium 1. 
METAL   291   291        Calcium 1. 
METAL   293   293        Calcium 1; via carbonyl oxygen. 
METAL   370   370        Calcium 2. 
METAL   374   374        Zinc; catalytic. 
METAL   378   378        Zinc; catalytic. 
METAL   398   398        Zinc; catalytic. 
METAL   409   409        Calcium 2. 
METAL   409   409        Calcium 3. 
METAL   415   415        Calcium 3; via carbonyl oxygen. 
METAL   417   417        Calcium 2. 
METAL   417   417        Calcium 3. 
METAL   419   419        Calcium 2; via carbonyl oxygen. 
METAL   422   422        Calcium 2. 
METAL   422   422        Calcium 3. 
METAL   425   425        Calcium 4; via carbonyl oxygen. 
METAL   426   426        Calcium 4. 
METAL   429   429        Calcium 4; via carbonyl oxygen. 
METAL   432   432        Calcium 4. 
CONFLICT   269   269        N -> D (in Ref. 2; AA sequence). 
CONFLICT   351   351        Q -> E (in Ref. 2; AA sequence). 
CONFLICT   400   400        I -> M (in Ref. 1; CAA54291). 
CONFLICT   409   409        E -> K (in Ref. 1; CAA54291). 
STRAND   236   243  8      
STRAND   249   264  16      
STRAND   271   275  5      
STRAND   280   283  4      
STRAND   288   294  7      
HELIX   297   299  3      
HELIX   300   320  21      
STRAND   332   337  6      
STRAND   339   341  3      
STRAND   345   347  3      
STRAND   349   354  6      
STRAND   359   363  5      
HELIX   365   367  3      
HELIX   369   383  15      
HELIX   391   411  21      
STRAND   418   421  4      
TURN   422   424  3      
STRAND   434   438  5      
HELIX   440   443  4      
HELIX   449   451  3      
HELIX   457   461  5      
TURN   462   465  4      
HELIX   466   478  13      
STRAND   480   482  3      
STRAND   485   487  3      
HELIX   492   505  14      
HELIX   513   528  16      
HELIX   533   545  13      
Sequence information
Length: 548 AA [This is the length of the unprocessed precursor] Molecular weight: 60104 Da [This is the MW of the unprocessed precursor] CRC64: 1D6ED3A545F045C8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKMKMKLASF GLAAGLAAQV FLPYNALAST EHVTWNQQFQ TPQFISGDLL KVNGTSPEEL 

        70         80         90        100        110        120 
VYQYVEKNEN KFKFHENAKD TLQLKEKKND NLGFTFMRFQ QTYKGIPVFG AVVTSHVKDG 

       130        140        150        160        170        180 
TLTALSGTLI PNLDTKGSLK SGKKLSEKQA RDIAEKDLVA NVTKEVPEYE QGKDTEFVVY 

       190        200        210        220        230        240 
VNGDEASLAY VVNLNFLTPE PGNWLYIIDA VDGKILNKFN QLDAAKPGDV KSITGTSTVG 

       250        260        270        280        290        300 
VGRGVLGDQK NINTTYSTYY YLQDNTRGNG IFTYDAKYRT TLPGSLWADA DNQFFASYDA 

       310        320        330        340        350        360 
PAVDAHYYAG VTYDYYKNVH NRLSYDGNNA AIRSSVHYSQ GYNNAFWNGS QMVYGDGDGQ 

       370        380        390        400        410        420 
TFIPLSGGID VVAHELTHAV TDYTAGLIYQ NESGAINEAI SDIFGTLVEF YANKNPDWEI 

       430        440        450        460        470        480 
GEDVYTPGIS GDSLRSMSDP AKYGDPDHYS KRYTGTQDNG GVHINSGIIN KAAYLISQGG 

       490        500        510        520        530        540 
THYGVSVVGI GRDKLGKIFY RALTQYLTPT SNFSQLRAAA VQSATDLYGS TSQEVASVKQ 


AFDAVGVK
P00800 in FASTA format

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