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UniProtKB/Swiss-Prot entry P00780


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SUBT_BACLI
Primary accession number P00780
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 83)
Name and origin of the protein
Protein name Subtilisin Carlsberg [Precursor]
Synonym EC 3.4.21.62
Gene name
Name: apr
From
Bacillus licheniformis [TaxID: 1402] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NCIMB 6816 / CCM 2182 / NCDO 727;
DOI=10.1093/nar/13.24.8913; PubMed=3001653 [NCBI, ExPASy, EBI, Israel, Japan]
Jacobs M., Eliasson M., Uhlen M., Flock J.-I.;
"Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis.";
Nucleic Acids Res. 13:8913-8926(1985).
[2]
PROTEIN SEQUENCE OF 106-379.
PubMed=4967581 [NCBI, ExPASy, EBI, Israel, Japan]
Smith E.L., Delange R.J., Evans W.H., Landon M., Markland F.S.;
"Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships.";
J. Biol. Chem. 243:2184-2191(1968).
[3]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT WITH SELENOCYSTEINE-325.
DOI=10.1021/bi00075a007; PubMed=8512925 [NCBI, ExPASy, EBI, Israel, Japan]
Syed R., Wu Z.P., Hogle J.M., Hilvert D.;
"Crystal structure of selenosubtilisin at 2.0-A resolution.";
Biochemistry 32:6157-6164(1993).
[4]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 106-379.
DOI=10.1021/bi971166o; PubMed=9425066 [NCBI, ExPASy, EBI, Israel, Japan]
Stoll V.S., Eger B.T., Hynes R.C., Martichonok V., Jones J.B., Pai E.F.;
"Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.";
Biochemistry 37:451-462(1998).
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.
  • SUBCELLULAR LOCATION: Secreted.
  • BIOTECHNOLOGY: Used as a detergent protease. Sold under the name Alcalase by Novozymes.
  • 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.
  • SIMILARITY: Belongs to the peptidase S8 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03341; CAB56500.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24111; SUBSCL.
3D structure databases
PDB
1AF4; X-ray; 2.60 A; A=106-379.[ExPASy / RCSB / EBI]
1AV7; X-ray; 2.60 A; A=106-379.[ExPASy / RCSB / EBI]
1AVT; X-ray; 2.00 A; A=106-379.[ExPASy / RCSB / EBI]
1BE6; X-ray; 2.15 A; A=106-379.[ExPASy / RCSB / EBI]
1BE8; X-ray; 2.20 A; A=106-379.[ExPASy / RCSB / EBI]
1BFK; X-ray; 2.30 A; A=106-379.[ExPASy / RCSB / EBI]
1BFU; X-ray; 2.20 A; A=106-379.[ExPASy / RCSB / EBI]
1C3L; X-ray; 2.16 A; A=106-379.[ExPASy / RCSB / EBI]
1CSE; X-ray; 1.20 A; E=106-379.[ExPASy / RCSB / EBI]
1OYV; X-ray; 2.50 A; A/B=106-379.[ExPASy / RCSB / EBI]
1R0R; X-ray; 1.10 A; E=106-379.[ExPASy / RCSB / EBI]
1SBC; X-ray; 2.50 A; A=106-379.[ExPASy / RCSB / EBI]
1SCA; X-ray; 2.00 A; A=106-379.[ExPASy / RCSB / EBI]
1SCB; X-ray; 2.30 A; A=106-379.[ExPASy / RCSB / EBI]
1SCD; X-ray; 2.30 A; A=106-379.[ExPASy / RCSB / EBI]
1SCN; X-ray; 1.90 A; E=106-379.[ExPASy / RCSB / EBI]
1SEL; X-ray; 2.00 A; A/B=106-379.[ExPASy / RCSB / EBI]
1VSB; X-ray; 2.10 A; A=106-379.[ExPASy / RCSB / EBI]
1YU6; X-ray; 1.55 A; A/B=106-379.[ExPASy / RCSB / EBI]
2SEC; X-ray; 1.80 A; E=106-379.[ExPASy / RCSB / EBI]
3VSB; X-ray; 2.60 A; A=106-379.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AF4; -.
1AV7; -.
1AVT; -.
1BE6; -.
1BE8; -.
1BFK; -.
1BFU; -.
1C3L; -.
1CSE; -.
1OYV; -.
1R0R; -.
1SBC; -.
1SCA; -.
1SCB; -.
1SCD; -.
1SCN; -.
1SEL; -.
1VSB; -.
1YU6; -.
2SEC; -.
3VSB; -.
ModBase P00780.
Protein family/group databases
MEROPS I09.001; -.
S08.001; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030435; Biological process: sporulation resulting in formation of a cellular spore (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000209; Pept_S8_S53.
IPR015500; Peptidase_S8_subtilisin-rel.
IPR010259; Prot_inh_S8A.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.200; Pept_S8_S53; 1.
PANTHER PTHR10795; SubtilSerProt; 1.
Pfam PF00082; Peptidase_S8; 1.
PF05922; Subtilisin_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00723; SUBTILISIN.
PROSITE PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.
BLOCKS P00780.
ProtoNet P00780.
Other
SWISS-3DIMAGE P00780.
LinkHub P00780; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Secreted; Serine protease; Signal; Sporulation; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    29  29     Potential. 
PROPEP   30   105  76      PRO_0000027179
CHAIN   106   379  274     Subtilisin Carlsberg. PRO_0000027180
ACT_SITE   137   137        By similarity. 
ACT_SITE   168   168        By similarity. 
ACT_SITE   325   325        By similarity. 
METAL   107   107        Calcium 1. 
METAL   146   146        Calcium 1. 
METAL   179   179        Calcium 1; via carbonyl oxygen. 
METAL   181   181        Calcium 1. 
METAL   185   185        Calcium 1; via carbonyl oxygen. 
METAL   273   273        Calcium 2; via carbonyl oxygen. 
METAL   275   275        Calcium 2; via carbonyl oxygen. 
METAL   278   278        Calcium 2; via carbonyl oxygen. 
CONFLICT   207   207        T -> S (in Ref. 2; AA sequence). 
CONFLICT   233   233        P -> A (in Ref. 2; AA sequence). 
CONFLICT   262   265        SSGN -> NSGS (in Ref. 2; AA sequence). 
CONFLICT   316   316        S -> N (in Ref. 2; AA sequence). 
HELIX   112   115  4      
HELIX   118   123  6      
STRAND   132   138  7      
STRAND   149   154  6      
STRAND   165   167  3      
HELIX   168   177  10      
STRAND   180   184  5      
STRAND   192   198  7      
STRAND   204   206  3      
HELIX   208   220  13      
STRAND   224   228  5      
STRAND   230   234  5      
HELIX   237   248  12      
STRAND   252   256  5      
TURN   272   274  3      
STRAND   278   284  7      
STRAND   300   305  6      
STRAND   307   313  7      
TURN   314   316  3      
STRAND   317   321  5      
HELIX   324   341  18      
HELIX   347   356  10      
HELIX   364   367  4      
HELIX   374   377  4      
Sequence information
Length: 379 AA [This is the length of the unprocessed precursor] Molecular weight: 38908 Da [This is the MW of the unprocessed precursor] CRC64: F19A6DC5761FB504 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMRKKSFWLG MLTAFMLVFT MAFSDSASAA QPAKNVEKDY IVGFKSGVKT ASVKKDIIKE 

        70         80         90        100        110        120 
SGGKVDKQFR IINAAKAKLD KEALKEVKND PDVAYVEEDH VAHALAQTVP YGIPLIKADK 

       130        140        150        160        170        180 
VQAQGFKGAN VKVAVLDTGI QASHPDLNVV GGASFVAGEA YNTDGNGHGT HVAGTVAALD 

       190        200        210        220        230        240 
NTTGVLGVAP SVSLYAVKVL NSSGSGTYSG IVSGIEWATT NGMDVINMSL GGPSGSTAMK 

       250        260        270        280        290        300 
QAVDNAYARG VVVVAAAGNS GSSGNTNTIG YPAKYDSVIA VGAVDSNSNR ASFSSVGAEL 

       310        320        330        340        350        360 
EVMAPGAGVY STYPTSTYAT LNGTSMASPH VAGAAALILS KHPNLSASQV RNRLSSTATY 

       370 
LGSSFYYGKG LINVEAAAQ 

P00780 in FASTA format

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View entry in raw text format (no links)
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