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P00800 (THER_BACTH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thermolysin
EC=3.4.24.27
Alternative name(s):
Thermostable neutral proteinase
Gene names
Name:npr
OrganismBacillus thermoproteolyticus
Taxonomic identifier1427 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Extracellular zinc metalloprotease.

Catalytic activity

Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.

Cofactor

Binds 4 calcium ions per subunit.

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M4 family.

Biophysicochemical properties

Temperature dependence:

Thermostable.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processextracellular matrix disassembly

Traceable author statement. Source: Reactome

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 By similarity
Propeptide29 – 232204Activation peptide
PRO_0000028592
Chain233 – 548316Thermolysin
PRO_0000028593

Sites

Active site3751 Ref.4
Active site4631Proton donor Ref.4
Metal binding2891Calcium 1
Metal binding2911Calcium 1
Metal binding2931Calcium 1; via carbonyl oxygen
Metal binding3701Calcium 2
Metal binding3741Zinc; catalytic
Metal binding3781Zinc; catalytic
Metal binding3981Zinc; catalytic
Metal binding4091Calcium 2
Metal binding4091Calcium 3
Metal binding4151Calcium 3; via carbonyl oxygen
Metal binding4171Calcium 2
Metal binding4171Calcium 3
Metal binding4191Calcium 2; via carbonyl oxygen
Metal binding4221Calcium 2
Metal binding4221Calcium 3
Metal binding4251Calcium 4; via carbonyl oxygen
Metal binding4261Calcium 4
Metal binding4291Calcium 4; via carbonyl oxygen
Metal binding4321Calcium 4

Experimental info

Sequence conflict2691N → D AA sequence Ref.2
Sequence conflict3511Q → E AA sequence Ref.2
Sequence conflict4001I → M in CAA54291. Ref.1
Sequence conflict4091E → K in CAA54291. Ref.1

Secondary structure

1 ......................................................... 548
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00800 [UniParc].

Last modified April 18, 2006. Version 3.
Checksum: 1D6ED3A545F045C8

FASTA54860,104
        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

« Hide

References

[1]"Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin."
O'Donohue M.J., Roques B.P., Beaumont A.
Biochem. J. 300:599-603(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Rokko.
[2]"Amino-acid sequence of thermolysin."
Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.
Nature New Biol. 238:35-37(1972)
Cited for: PROTEIN SEQUENCE OF 233-548.
[3]"Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide."
Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.
Biochemistry 11:2427-2435(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 233-268; 352-400 AND 438-477.
[4]"Evidence of an essential histidine residue in thermolysin."
Burstein Y., Walsh K.A., Neurath H.
Biochemistry 13:205-210(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[5]"Structure of thermolysin refined at 1.6-A resolution."
Holmes M.A., Matthews B.W.
J. Mol. Biol. 160:623-639(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[6]"The conformation of thermolysin."
Matthews B.W., Weaver L.H., Kester W.R.
J. Biol. Chem. 249:8030-8044(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[7]"NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure."
Rico M., Jimenez M.A., Gonzalez C., de Filippis V., Fontana A.
Biochemistry 33:14834-14847(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 487-548.
[8]"NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding."
Conejero-Lara F., Gonzalez C., Jimenez M.A., Padmanabhan S., Mateo P.L., Rico M.
Biochemistry 36:11975-11983(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 437-548.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76986 Genomic DNA. Translation: CAA54291.1.
PIRHYBST. I40579.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJ3X-ray2.00A233-548[»]
1FJOX-ray2.00A233-548[»]
1FJQX-ray1.70A233-548[»]
1FJTX-ray2.20A233-548[»]
1FJUX-ray2.00A233-548[»]
1FJVX-ray2.00A233-548[»]
1FJWX-ray1.90A233-548[»]
1GXWX-ray2.18A233-548[»]
1HYTX-ray1.70A233-548[»]
1KEIX-ray1.60A233-548[»]
1KJOX-ray1.60A233-548[»]
1KJPX-ray1.60A233-548[»]
1KKKX-ray1.60A233-548[»]
1KL6X-ray1.80A233-548[»]
1KR6X-ray1.80A233-548[»]
1KROX-ray1.70A233-548[»]
1KS7X-ray1.70A233-548[»]
1KTOX-ray1.90A233-548[»]
1L3FX-ray2.30E233-548[»]
1LNAX-ray1.90E233-548[»]
1LNBX-ray1.80E233-548[»]
1LNCX-ray1.80E233-548[»]
1LNDX-ray1.70E233-548[»]
1LNEX-ray1.70E233-548[»]
1LNFX-ray1.70E233-548[»]
1OS0X-ray2.10A233-548[»]
1PE5X-ray1.70A233-548[»]
1PE7X-ray1.82A233-548[»]
1PE8X-ray1.80A233-548[»]
1QF0X-ray2.20A233-548[»]
1QF1X-ray2.00A233-548[»]
1QF2X-ray2.06A233-548[»]
1THLX-ray1.70A233-548[»]
1TLIX-ray2.05A233-548[»]
1TLPX-ray2.30E233-548[»]
1TLXX-ray2.10A233-548[»]
1TMNX-ray1.90E233-548[»]
1TRLNMR-A/B487-548[»]
1Y3GX-ray2.10E233-548[»]
1Z9GX-ray1.70E233-548[»]
1ZDPX-ray1.70E233-548[»]
2A7GX-ray1.85E233-548[»]
2G4ZX-ray1.98A233-548[»]
2TLIX-ray1.95A233-548[»]
2TLXX-ray1.65A233-548[»]
2TMNX-ray1.60E233-548[»]
2WHZX-ray1.75A233-548[»]
2WI0X-ray1.95A233-548[»]
3DNZX-ray1.20A233-548[»]
3DO0X-ray1.36A233-548[»]
3DO1X-ray1.33A233-548[»]
3DO2X-ray1.22A233-548[»]
3EIMX-ray1.88A233-548[»]
3F28X-ray1.68A233-548[»]
3F2PX-ray1.95A233-548[»]
3FB0X-ray1.60A233-548[»]
3FBOX-ray1.92A233-548[»]
3FCQX-ray1.75A233-548[»]
3FGDX-ray1.33A233-548[»]
3FLFX-ray1.97A233-548[»]
3FORX-ray1.93A233-548[»]
3FV4X-ray1.56A233-548[»]
3FVPX-ray1.41A233-548[»]
3FXPX-ray2.05A233-548[»]
3FXSX-ray1.55A233-548[»]
3LS7X-ray1.98A233-548[»]
3MS3X-ray1.54A233-548[»]
3MSAX-ray1.66A233-548[»]
3MSFX-ray2.09A233-548[»]
3MSNX-ray1.97A233-548[»]
3N21X-ray1.87A233-548[»]
3NN7X-ray2.05A233-548[»]
3P7PX-ray2.20E233-548[»]
3P7QX-ray2.20E233-548[»]
3P7RX-ray2.20E233-548[»]
3P7SX-ray2.20E233-548[»]
3P7TX-ray2.20E233-548[»]
3P7UX-ray2.20E233-548[»]
3P7VX-ray2.20E233-548[»]
3P7WX-ray2.20E233-548[»]
3QGOX-ray1.45A233-548[»]
3QH1X-ray1.55A233-548[»]
3QH5X-ray1.50A233-548[»]
3SSBX-ray1.80A/B233-548[»]
3T2HX-ray1.95E233-548[»]
3T2IX-ray2.10E233-548[»]
3T2JX-ray2.00E233-548[»]
3T73X-ray1.60A233-548[»]
3T74X-ray1.28A233-548[»]
3T87X-ray1.28A233-548[»]
3T8CX-ray1.66A233-548[»]
3T8DX-ray1.41A233-548[»]
3T8FX-ray1.44A233-548[»]
3T8GX-ray1.50A233-548[»]
3T8HX-ray1.45A233-548[»]
3TLIX-ray1.95A233-548[»]
3TMNX-ray1.70E233-548[»]
4D91X-ray1.90A233-548[»]
4D9WX-ray1.38A233-548[»]
4H57X-ray1.56A233-548[»]
4TLIX-ray1.95A233-548[»]
4TLNX-ray2.30A233-548[»]
4TMNX-ray1.70E233-548[»]
5TLIX-ray2.10A233-548[»]
5TLNX-ray2.30A233-548[»]
5TMNX-ray1.60E233-548[»]
6TLIX-ray2.10A233-548[»]
6TMNX-ray1.60E233-548[»]
7TLIX-ray1.95A233-548[»]
7TLNX-ray2.30A233-548[»]
8TLIX-ray2.20A233-548[»]
8TLNX-ray1.60E233-548[»]
ProteinModelPortalP00800.
SMRP00800. Positions 233-548.
ModBaseSearch...

Protein family/group databases

MEROPSM04.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Family and domain databases

Gene3D3.10.170.10. 1 hit.
InterProIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSPR00730. THERMOLYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP00800.
ChEMBLCHEMBL3392.
EvolutionaryTraceP00800.

Entry information

Entry nameTHER_BACTH
AccessionPrimary (citable) accession number: P00800
Secondary accession number(s): Q45779
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 18, 2006
Last modified: April 3, 2013
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents