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Reviewed, UniProtKB/Swiss-Prot P29142 (SUBT_BACST)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Subtilisin J
    EC=3.4.21.62
Gene names
Name: aprJ
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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 2 calcium ions per subunit By similarity.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Propeptide30 – 10677 Potential
PRO_0000027185
Chain107 – 381275Subtilisin J
PRO_0000027186

Sites

Active site1381Charge relay system By similarity
Active site1701Charge relay system By similarity
Active site3271Charge relay system By similarity
Metal binding1081Calcium 1 By similarity
Metal binding1471Calcium 1 By similarity
Metal binding1811Calcium 1; via carbonyl oxygen By similarity
Metal binding1831Calcium 1 By similarity
Metal binding1851Calcium 1; via carbonyl oxygen By similarity
Metal binding1871Calcium 1; via carbonyl oxygen By similarity
Metal binding2751Calcium 2; via carbonyl oxygen By similarity
Metal binding2771Calcium 2; via carbonyl oxygen By similarity
Metal binding2801Calcium 2; via carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
P29142-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: C7A596F7629087D5

FASTA38139,495
        10         20         30         40         50         60 
MRSKKLWISL LFALTLIFTM AFSNMSVQAA GKSSTEKKYI VGFKQTMSAM SSAKKKDVIS 

        70         80         90        100        110        120 
EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED HIAHEYAQSV PYGISQIKAP 

       130        140        150        160        170        180 
ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV RGGASFVPSE TNPYQDGSSH GTHVAGTIAA 

       190        200        210        220        230        240 
LNNSIGVLGV SPSASLYAVK VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPSGSTA 

       250        260        270        280        290        300 
LKTVVDKAVS SGIVVAAAAG NEGSSGSSST VGYPAKYPST IAVGAVNSSN QRASFSSAGS 

       310        320        330        340        350        360 
ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTA 

       370        380 
TYLGNSFYYG KGLINVQAAA Q

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References

[1]"Molecular cloning of a subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis."
Jang J.S., Kang D.O., Chun M.J., Byun S.M.
Biochem. Biophys. Res. Commun. 184:277-282(1992) [PubMed: 1567435] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 2313 / NCIB 10278 / KCTC 1823.

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Cross-references

Sequence databases

M64743 Genomic DNA. Translation: AAA22247.1.
PIRJQ1487.

3D structure databases

HSSPHSSP built from PDB template 1SCJ based on UniProtKB P04189.
SMRP29142. Positions 36-106, 107-381.
ModBaseSearch...

Protein family/group databases

MEROPSI09.001.
S08.035.

Enzyme and pathway databases

BRENDA3.4.21.62. 266715.

Family and domain databases

InterProIPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR010259. Prot_inh_S8A.
[Graphical view]
Gene3DG3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHERPTHR10795. SubtilSerProt. 1 hit.
PfamPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSUBT_BACST
AccessionPrimary (citable) accession number: P29142
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents