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Protein

Subtilisin Savinase

Gene
N/A
Organism
Bacillus lentus
Status
Reviewed-Annotation score: 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

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2 – 21Calcium 1
Active sitei32 – 321Charge relay system
Metal bindingi40 – 401Calcium 1
Active sitei62 – 621Charge relay system
Metal bindingi73 – 731Calcium 1; via carbonyl oxygen
Metal bindingi75 – 751Calcium 1
Metal bindingi77 – 771Calcium 1; via carbonyl oxygen
Metal bindingi79 – 791Calcium 1; via carbonyl oxygen
Metal bindingi163 – 1631Calcium 2; via carbonyl oxygen
Metal bindingi165 – 1651Calcium 2; via carbonyl oxygen
Metal bindingi168 – 1681Calcium 2; via carbonyl oxygen
Active sitei215 – 2151Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.62. 668.

Protein family/group databases

MEROPSiS08.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin Savinase (EC:3.4.21.62)
Alternative name(s):
Alkaline protease
OrganismiBacillus lentus
Taxonomic identifieri1467 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

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

Protein family/group databases

Allergomei903. Bac l Subtilisin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Subtilisin SavinasePRO_0000076418Add
BLAST

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 105Combined sources
Helixi13 – 186Combined sources
Beta strandi27 – 337Combined sources
Beta strandi43 – 486Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 613Combined sources
Helixi62 – 7110Combined sources
Beta strandi75 – 784Combined sources
Beta strandi87 – 926Combined sources
Beta strandi98 – 1003Combined sources
Helixi102 – 11413Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi126 – 1283Combined sources
Helixi131 – 14212Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi156 – 1583Combined sources
Turni162 – 1643Combined sources
Beta strandi168 – 1747Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi197 – 2037Combined sources
Turni204 – 2063Combined sources
Beta strandi207 – 2115Combined sources
Helixi214 – 23118Combined sources
Helixi237 – 24610Combined sources
Helixi254 – 2574Combined sources
Helixi264 – 2674Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9JX-ray1.80A1-267[»]
1C9MX-ray1.67A1-269[»]
1C9NX-ray1.50A1-267[»]
1GCIX-ray0.78A1-269[»]
1IAVX-ray1.80A1-269[»]
1JEAX-ray2.00A1-269[»]
1NDQX-ray1.80A1-269[»]
1NDUX-ray1.60A1-269[»]
1Q5PX-ray1.60A1-269[»]
1SVNX-ray1.40A1-269[»]
1TK2X-ray1.54A1-263[»]
3BX1X-ray1.85A/B1-269[»]
4CFYX-ray1.17A1-269[»]
4CFZX-ray1.57A1-269[»]
4CG0X-ray1.36A1-269[»]
5AQEX-ray1.10A1-269[»]
ProteinModelPortaliP29600.
SMRiP29600. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29600.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 268242Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AQSVPWGISR VQAPAAHNRG LTGSGVKVAV LDTGISTHPD LNIRGGASFV
60 70 80 90 100
PGEPSTQDGN GHGTHVAGTI AALNNSIGVL GVAPSAELYA VKVLGASGSG
110 120 130 140 150
SVSSIAQGLE WAGNNGMHVA NLSLGSPSPS ATLEQAVNSA TSRGVLVVAA
160 170 180 190 200
SGNSGAGSIS YPARYANAMA VGATDQNNNR ASFSQYGAGL DIVAPGVNVQ
210 220 230 240 250
STYPGSTYAS LNGTSMATPH VAGAAALVKQ KNPSWSNVQI RNHLKNTATS
260
LGSTNLYGSG LVNAEAATR
Length:269
Mass (Da):26,698
Last modified:April 1, 1993 - v1
Checksum:i4D89F8778999BF8D
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9JX-ray1.80A1-267[»]
1C9MX-ray1.67A1-269[»]
1C9NX-ray1.50A1-267[»]
1GCIX-ray0.78A1-269[»]
1IAVX-ray1.80A1-269[»]
1JEAX-ray2.00A1-269[»]
1NDQX-ray1.80A1-269[»]
1NDUX-ray1.60A1-269[»]
1Q5PX-ray1.60A1-269[»]
1SVNX-ray1.40A1-269[»]
1TK2X-ray1.54A1-263[»]
3BX1X-ray1.85A/B1-269[»]
4CFYX-ray1.17A1-269[»]
4CFZX-ray1.57A1-269[»]
4CG0X-ray1.36A1-269[»]
5AQEX-ray1.10A1-269[»]
ProteinModelPortaliP29600.
SMRiP29600. Positions 1-269.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei903. Bac l Subtilisin.
MEROPSiS08.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.62. 668.

Miscellaneous databases

EvolutionaryTraceiP29600.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4-A resolution."
    Betzel C., Klupsch S., Papendorf G., Hastrup S., Branner S., Wilson K.S.
    J. Mol. Biol. 223:427-445(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
  2. "Backbone dynamics of the 269-residue protease Savinase determined from 15N-NMR relaxation measurements."
    Remerowski M.L., Pepermans H.A.M., Hilbers C.W., van de Ven F.J.M.
    Eur. J. Biochem. 235:629-640(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  3. "The 0.78-A structure of a serine protease: Bacillus lentus subtilisin."
    Kuhn P., Knapp M., Soltis S.M., Ganshaw G., Thoene M., Bott R.
    Biochemistry 37:13446-13452(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.78 ANGSTROMS).

Entry informationi

Entry nameiSUBS_BACLE
AccessioniPrimary (citable) accession number: P29600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 9, 2015
This is version 104 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.