SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00780

- SUBT_BACLI

UniProt

P00780 - SUBT_BACLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Subtilisin Carlsberg

Gene
apr
Organism
Bacillus licheniformis
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Calcium 1
Active sitei137 – 1371 By similarity
Metal bindingi146 – 1461Calcium 1
Active sitei168 – 1681 By similarity
Metal bindingi179 – 1791Calcium 1; via carbonyl oxygen
Metal bindingi181 – 1811Calcium 1
Metal bindingi185 – 1851Calcium 1; via carbonyl oxygen
Metal bindingi273 – 2731Calcium 2; via carbonyl oxygen
Metal bindingi275 – 2751Calcium 2; via carbonyl oxygen
Metal bindingi278 – 2781Calcium 2; via carbonyl oxygen
Active sitei325 – 3251 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiI09.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin Carlsberg (EC:3.4.21.62)
Gene namesi
Name:apr
OrganismiBacillus licheniformis
Taxonomic identifieri1402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Used as a detergent protease. Sold under the name Alcalase by Novozymes.

Protein family/group databases

Allergomei8254. Bac li Subtilisin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 By similarityAdd
BLAST
Propeptidei30 – 10576PRO_0000027179Add
BLAST
Chaini106 – 379274Subtilisin CarlsbergPRO_0000027180Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Protein-protein interaction databases

IntActiP00780. 2 interactions.
MINTiMINT-1505000.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi112 – 1154
Helixi118 – 1236
Beta strandi132 – 1387
Beta strandi149 – 1546
Beta strandi156 – 1583
Beta strandi161 – 1633
Beta strandi165 – 1673
Helixi168 – 17710
Beta strandi180 – 1845
Beta strandi192 – 1987
Beta strandi204 – 2063
Helixi208 – 22013
Beta strandi224 – 2285
Beta strandi230 – 2345
Helixi237 – 24812
Beta strandi252 – 2565
Turni272 – 2743
Beta strandi278 – 2847
Beta strandi300 – 3056
Beta strandi307 – 3137
Turni314 – 3163
Beta strandi317 – 3215
Helixi324 – 34118
Helixi347 – 35610
Helixi364 – 3674
Helixi374 – 3774

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AF4X-ray2.60A106-379[»]
1AV7X-ray2.60A106-379[»]
1AVTX-ray2.00A106-379[»]
1BE6X-ray2.15A106-379[»]
1BE8X-ray2.20A106-379[»]
1BFKX-ray2.30A106-379[»]
1BFUX-ray2.20A106-379[»]
1C3LX-ray2.16A106-378[»]
1CSEX-ray1.20E106-379[»]
1OYVX-ray2.50A/B106-379[»]
1R0RX-ray1.10E106-378[»]
1SBCX-ray2.50A106-379[»]
1SCAX-ray2.00A106-379[»]
1SCBX-ray2.30A106-379[»]
1SCDX-ray2.30A106-379[»]
1SCNX-ray1.90E106-379[»]
1SELX-ray2.00A/B106-379[»]
1VSBX-ray2.10A106-379[»]
1YU6X-ray1.55A/B106-379[»]
2SECX-ray1.80E106-379[»]
2WUVX-ray2.24A106-379[»]
2WUWX-ray2.23E106-379[»]
3UNXX-ray1.26A106-379[»]
3VSBX-ray2.60A106-379[»]
ProteinModelPortaliP00780.
SMRiP00780. Positions 37-104, 106-379.

Miscellaneous databases

EvolutionaryTraceiP00780.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S8 family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00780-1 [UniParc]FASTAAdd to Basket

« Hide

MMRKKSFWLG MLTAFMLVFT MAFSDSASAA QPAKNVEKDY IVGFKSGVKT    50
ASVKKDIIKE SGGKVDKQFR IINAAKAKLD KEALKEVKND PDVAYVEEDH 100
VAHALAQTVP YGIPLIKADK VQAQGFKGAN VKVAVLDTGI QASHPDLNVV 150
GGASFVAGEA YNTDGNGHGT HVAGTVAALD NTTGVLGVAP SVSLYAVKVL 200
NSSGSGTYSG IVSGIEWATT NGMDVINMSL GGPSGSTAMK QAVDNAYARG 250
VVVVAAAGNS GSSGNTNTIG YPAKYDSVIA VGAVDSNSNR ASFSSVGAEL 300
EVMAPGAGVY STYPTSTYAT LNGTSMASPH VAGAAALILS KHPNLSASQV 350
RNRLSSTATY LGSSFYYGKG LINVEAAAQ 379
Length:379
Mass (Da):38,908
Last modified:August 1, 1988 - v1
Checksum:iF19A6DC5761FB504
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071T → S AA sequence 1 Publication
Sequence conflicti233 – 2331P → A AA sequence 1 Publication
Sequence conflicti262 – 2654SSGN → NSGS AA sequence 1 Publication
Sequence conflicti316 – 3161S → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03341 Genomic DNA. Translation: CAB56500.1.
PIRiA24111. SUBSCL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03341 Genomic DNA. Translation: CAB56500.1 .
PIRi A24111. SUBSCL.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AF4 X-ray 2.60 A 106-379 [» ]
1AV7 X-ray 2.60 A 106-379 [» ]
1AVT X-ray 2.00 A 106-379 [» ]
1BE6 X-ray 2.15 A 106-379 [» ]
1BE8 X-ray 2.20 A 106-379 [» ]
1BFK X-ray 2.30 A 106-379 [» ]
1BFU X-ray 2.20 A 106-379 [» ]
1C3L X-ray 2.16 A 106-378 [» ]
1CSE X-ray 1.20 E 106-379 [» ]
1OYV X-ray 2.50 A/B 106-379 [» ]
1R0R X-ray 1.10 E 106-378 [» ]
1SBC X-ray 2.50 A 106-379 [» ]
1SCA X-ray 2.00 A 106-379 [» ]
1SCB X-ray 2.30 A 106-379 [» ]
1SCD X-ray 2.30 A 106-379 [» ]
1SCN X-ray 1.90 E 106-379 [» ]
1SEL X-ray 2.00 A/B 106-379 [» ]
1VSB X-ray 2.10 A 106-379 [» ]
1YU6 X-ray 1.55 A/B 106-379 [» ]
2SEC X-ray 1.80 E 106-379 [» ]
2WUV X-ray 2.24 A 106-379 [» ]
2WUW X-ray 2.23 E 106-379 [» ]
3UNX X-ray 1.26 A 106-379 [» ]
3VSB X-ray 2.60 A 106-379 [» ]
ProteinModelPortali P00780.
SMRi P00780. Positions 37-104, 106-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00780. 2 interactions.
MINTi MINT-1505000.

Chemistry

BindingDBi P00780.
ChEMBLi CHEMBL4299.

Protein family/group databases

Allergomei 8254. Bac li Subtilisin.
MEROPSi I09.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P00780.

Family and domain databases

Gene3Di 3.40.50.200. 1 hit.
InterProi IPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view ]
PANTHERi PTHR10795. PTHR10795. 1 hit.
Pfami PF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view ]
PRINTSi PR00723. SUBTILISIN.
SUPFAMi SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEi PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis."
    Jacobs M., Eliasson M., Uhlen M., Flock J.-I.
    Nucleic Acids Res. 13:8913-8926(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCIMB 6816 / CCM 2182 / NCDO 727.
  2. "Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships."
    Smith E.L., Delange R.J., Evans W.H., Landon M., Markland F.S.
    J. Biol. Chem. 243:2184-2191(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 106-379.
  3. "Crystal structure of selenosubtilisin at 2.0-A resolution."
    Syed R., Wu Z.P., Hogle J.M., Hilvert D.
    Biochemistry 32:6157-6164(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT WITH SELENOCYSTEINE-325.
  4. "Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes."
    Stoll V.S., Eger B.T., Hynes R.C., Martichonok V., Jones J.B., Pai E.F.
    Biochemistry 37:451-462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 106-379.

Entry informationi

Entry nameiSUBT_BACLI
AccessioniPrimary (citable) accession number: P00780
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi