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P06874 (NPRT_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thermostable neutral protease NprT
EC=3.4.24.-
Alternative name(s):
Thermostable neutral proteinase
Gene names
Name:nprT
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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. Ref.2

Cofactor

Binds 4 calcium ions per subunit Probable. Ref.2

Binds 1 zinc ion per subunit Probable. Ref.2

Enzyme regulation

Its casein hydrolytic activity is inhibited almost completely by a chelating agent (EDTA), whereas neither diisopropyl fluorophosphate nor phenylmethylsulfonyl fluoride inhibit the proteolytic activity in vitro.

Subcellular location

Secreted Ref.2.

Sequence similarities

Belongs to the peptidase M4 family.

Biophysicochemical properties

pH dependence:

Optimum pH is about 7. Ref.2

Temperature dependence:

Thermostable. Retains about 80% of its activity after treatment of 65 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)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 229204Activation peptide
PRO_0000028590
Chain230 – 548319Thermostable neutral protease NprT
PRO_0000028591

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P06874 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 5B4D2C1D7910539D

FASTA54859,580
        10         20         30         40         50         60 
MNKRAMLGAI GLAFGLLAAP IGASAKGESI VWNEQWKTPS FVSGSLLNGG EQALEELVYQ 

        70         80         90        100        110        120 
YVDRENGTFR LGGRARDRLA LIGKQTDELG HTVMRFEQRH HGIPVYGTML AAHVKDGELI 

       130        140        150        160        170        180 
ALSGSLIPNL DGQPRLKKAK TVTVQQAEAI AEQDVTETVT KERPTTENGE RTRLVIYPTD 

       190        200        210        220        230        240 
GTARLAYEVN VRFLTPVPGN WVYIIDATDG AILNKFNQID SRQPGGGQPV AGASTVGVGR 

       250        260        270        280        290        300 
GVLGDQKYIN TTYSSYYGYY YLQDNTRGSG IFTYDGRNRT VLPGSLWTDG DNQFTASYDA 

       310        320        330        340        350        360 
AAVDAHYYAG VVYDYYKNVH GRLSYDGSNA AIRSTVHYGR GYNNAFWNGS QMVYGDGDGQ 

       370        380        390        400        410        420 
TFLPFSGGID VVGHELTHAV TDYTAGLVYQ NESGAINEAM SDIFGTLVEF YANRNPDWEI 

       430        440        450        460        470        480 
GEDIYTPGVA GDALRSMSDP AKYGDPDHYS KRYTGTQDNG GVHTNSGIIN KAAYLLSQGG 

       490        500        510        520        530        540 
VHYGVSVNGI GRDKMGKIFY RALVYYLTPT SNFSQLRAAC VQAAADLYGS TSQEVNSVKQ 


AFNAVGVY

« Hide

References

[1]"Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus."
Takagi M., Imanaka T., Aiba S.
J. Bacteriol. 163:824-831(1985) [PubMed: 2993245] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 230-243, DETERMINATION OF TRANSCRIPTIONAL START SITE.
Strain: CU21.
[2]"Molecular cloning of a thermostable neutral protease gene from Bacillus stearothermophilus in a vector plasmid and its expression in Bacillus stearothermophilus and Bacillus subtilis."
Fujii M., Takagi M., Imanaka T., Aiba S.
J. Bacteriol. 154:831-837(1983) [PubMed: 6302083] [Abstract]
Cited for: FUNCTION AS A PROTEASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Strain: CU21.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M11446 Genomic DNA. Translation: AAA22621.1.
PIRHYBSS. A24924.

3D structure databases

ProteinModelPortalP06874.
SMRP06874. Positions 230-547.
ModBaseSearch...

Protein family/group databases

MEROPSM04.018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011096. FTP_domain.
IPR005075. Pept_M4_propep_PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
Gene3DG3DSA:3.10.170.10. Peptidase_M4. 1 hit.
G3DSA:1.10.390.10. Peptidase_M4/M36. 1 hit.
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 nameNPRT_GEOSE
AccessionPrimary (citable) accession number: P06874
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 25, 2012
This is version 88 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

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