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P43133 (THER_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Thermolysin

EC=3.4.24.27
Alternative name(s):
Neutral protease
Gene names
Name:nprS
Synonyms:nprM
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length551 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. Ref.1

Catalytic activity

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

Cofactor

Binds 4 calcium ions per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted Ref.1.

Induction

Is expressed in the stationary phase. Up-regulated by NprA. Ref.2

Sequence similarities

Belongs to the peptidase M4 family.

Biophysicochemical properties

Temperature dependence:

Thermostable. Retains about 45% of its activity after treatment of 90 degrees Celsius for 30 minutes.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 3131 Potential
Propeptide32 – 235204Activation peptide
PRO_0000028612
Chain236 – 551316Thermolysin
PRO_0000028613

Sites

Active site3781 By similarity
Active site4661Proton donor By similarity
Metal binding2921Calcium 1 By similarity
Metal binding2941Calcium 1 By similarity
Metal binding2961Calcium 1; via carbonyl oxygen By similarity
Metal binding3731Calcium 2 By similarity
Metal binding3771Zinc; catalytic By similarity
Metal binding3811Zinc; catalytic By similarity
Metal binding4011Zinc; catalytic By similarity
Metal binding4121Calcium 2 By similarity
Metal binding4121Calcium 3 By similarity
Metal binding4181Calcium 3; via carbonyl oxygen By similarity
Metal binding4201Calcium 2 By similarity
Metal binding4201Calcium 3 By similarity
Metal binding4221Calcium 2; via carbonyl oxygen By similarity
Metal binding4251Calcium 2 By similarity
Metal binding4251Calcium 3 By similarity
Metal binding4291Calcium 4 By similarity
Metal binding4321Calcium 4; via carbonyl oxygen By similarity
Metal binding4351Calcium 4 By similarity

Experimental info

Sequence conflict10 – 145VRFGL → RSFGV AA sequence Ref.2
Sequence conflict241Missing in AAB02774. Ref.2
Sequence conflict29 – 335ALAST → RLASS AA sequence Ref.2
Sequence conflict1141A → Q in AAB02774. Ref.2
Sequence conflict1241T → S in AAB02774. Ref.2
Sequence conflict1341P → PIP AA sequence Ref.2
Sequence conflict2611T → S in AAB02774. Ref.2
Sequence conflict4631G → A in AAB02774. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P43133 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FCF4B2B5A7870129

FASTA55160,617
        10         20         30         40         50         60 
MKRKMKMKLV RFGLAAGLAA QVFFLPYNAL ASTEHVTWNQ QFQTPQFISG DLLKVNGTSP 

        70         80         90        100        110        120 
EELVYQYVEK NENKFKFHEN AKDTLQLKEK KNDNLGFTFM RFQQTYKGIP VFGAVVTAHV 

       130        140        150        160        170        180 
KDGTLTALSG TLIPNLDTKG SLKSGKKLSE KQARDIAEKD LVANVTKEVP EYEQGKDTEF 

       190        200        210        220        230        240 
VVYVNGDEAS LAYVVNLNFL TPEPGNWLYI IDAVDGKILN KFNQLDAAKP GDVKSITGTS 

       250        260        270        280        290        300 
TVGVGRGVLG DQKNINTTYS TYYYLQDNTR GNGIFTYDAK YRTTLPGSLW ADADNQFFAS 

       310        320        330        340        350        360 
YDAPAVDAHY YAGVTYDYYK NVHNRLSYDG NNAAIRSSVH YSQGYNNAFW NGSQMVYGDG 

       370        380        390        400        410        420 
DGQTFIPLSG GIDVVAHELT HAVTDYTAGL IYQNESGAIN EAISDIFGTL VEFYANKNPD 

       430        440        450        460        470        480 
WEIGEDVYTP GISGDSLRSM SDPAKYGDPD HYSKRYTGTQ DNGGVHINSG IINKAAYLIS 

       490        500        510        520        530        540 
QGGTHYGVSV VGIGRDKLGK IFYRALTQYL TPTSNFSQLR AAAVQSATDL YGSTSQEVAS 

       550 
VKQAFDAVGV K 

« Hide

References

[1]"Cloning and nucleotide sequence of the highly thermostable neutral protease gene from Bacillus stearothermophilus."
Kubo M., Imanaka T.
J. Gen. Microbiol. 134:1883-1892(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 236-240, FUNCTION AS A PROTEASE, TEMPERATURE DEPENDENCE, SUBCELLULAR LOCATION.
Strain: MK232.
[2]"Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene."
Nishiya Y., Imanaka T.
J. Bacteriol. 172:4861-4869(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 236-239, INDUCTION.
Strain: TELNE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21663 Genomic DNA. Translation: AAB02774.1.
M34237 Genomic DNA. Translation: AAA22625.1.
PIRA46564.
B36706.

3D structure databases

ProteinModelPortalP43133.
SMRP43133. Positions 236-551.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB01093. Dimethyl sulfoxide.

Protein family/group databases

MEROPSM04.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameTHER_GEOSE
AccessionPrimary (citable) accession number: P43133
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries