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P28842 (SUBT_BACS9) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. 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:
Subtilisin

EC=3.4.21.62
Gene names
Name:sub1
OrganismBacillus sp. (strain TA39)
Taxonomic identifier29336 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

Catalytic activity

Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

Cofactor

Binds 1 calcium ion per subunit Potential.

Subcellular location

Secreted.

Miscellaneous

Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.

Sequence similarities

Belongs to the peptidase S8 family.

Biophysicochemical properties

Temperature dependence:

Still active at temperatures close to 0 degrees Celsius. Thermolabile.

Ontologies

Keywords
   Biological processSporulation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMZymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase 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 – 11180 Potential
PRO_0000027181
Chain112 – 420309Subtilisin
PRO_0000027182

Sites

Active site1451Charge relay system By similarity
Active site1821Charge relay system By similarity
Active site3601Charge relay system By similarity
Metal binding1151Calcium Potential
Metal binding1541Calcium Potential

Sequences

Sequence LengthMass (Da)Tools
P28842 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: AE4F121BD32B26EC

FASTA42044,087
        10         20         30         40         50         60 
MKRSGKIFTT AMLAVTLMMP AMGVSANEGN AAAEGNEKFR VLVDSVDQKN LKNAKQQYGV 

        70         80         90        100        110        120 
HWDFAGEGFT TDMNEKQFNA LKKNKNLTVE KVPELEIATA TDKPEALYNA MAASQSTPWG 

       130        140        150        160        170        180 
IKAIYNNSSI TQTSGGGGIN IAVLDTGVNT NHPDLRNNVE QCKDFTVGTT YTNNSCTDRQ 

       190        200        210        220        230        240 
GHGTHVAGSA LADGGTGNGV YGVAPDADLW AYKVLGDDGS GYADDIAAAI RHAGDQATAL 

       250        260        270        280        290        300 
NTKVVINMSL GSSGESSLIT NAVNYSYNKG VLIIAAAGNS GPYQGSIGYP GALVNAVAVA 

       310        320        330        340        350        360 
ALENKVENGT YRVADFSSRG YSWTDGDYAI QKGDVEISAP GAAIYSTWFD GGYATISGTS 

       370        380        390        400        410        420 
MASPHAAGLA AKIWAQYPSA SNVDVRGELQ YRAYENDILS GYYAGYGDDF ASGFGFATVQ 

« Hide

References

[1]"Nucleotide and derived amino acid sequence of the subtilisin from the antarctic psychrotroph Bacillus TA39."
Narinx E., Davail S., Feller G., Gerday C.
Biochim. Biophys. Acta 1131:111-113(1992) [PubMed: 1581352] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62369 Genomic DNA. Translation: CAA44227.1.
PIRS23407.

3D structure databases

ProteinModelPortalP28842.
SMRP28842. Positions 112-420.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000209. Peptidase_S8/S53.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
Gene3DG3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHERPTHR10795. SubtilSerProt. 1 hit.
PfamPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF52743. Pept_S8_S53. 1 hit.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUBT_BACS9
AccessionPrimary (citable) accession number: P28842
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 16, 2011
This is version 74 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