Reviewed, UniProtKB/Swiss-Prot P29600 (SUBS_BACLE)

Names and origin

Protein names	Recommended name:     Subtilisin Savinase     EC=3.4.21.62 Alternative name(s):     Alkaline protease
Organism	Bacillus lentus
Taxonomic identifier	1467 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 2 calcium ions per subunit.
Subcellular location	Secreted.
Biotechnological use	Used as a detergent protease. Sold under the name Savinase 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.
Sequence similarities	Belongs to the peptidase S8 family.

Ontologies

Keywords
Biological process	Sporulation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 269

269

Subtilisin Savinase

PRO_0000076418

Sites

Active site

32

1

Charge relay system

Active site

62

1

Charge relay system

Active site

215

1

Charge relay system

Metal binding

2

1

Calcium 1

Metal binding

40

1

Calcium 1

Metal binding

73

1

Calcium 1; via carbonyl oxygen

Metal binding

75

1

Calcium 1

Metal binding

77

1

Calcium 1; via carbonyl oxygen

Metal binding

79

1

Calcium 1; via carbonyl oxygen

Metal binding

163

1

Calcium 2; via carbonyl oxygen

Metal binding

165

1

Calcium 2; via carbonyl oxygen

Metal binding

168

1

Calcium 2; via carbonyl oxygen

Secondary structure

1

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269

Helix Strand Turn

Details...

Helix

6 – 10

5

Helix

13 – 18

6

Beta strand

27 – 33

7

Beta strand

43 – 48

6

Beta strand

59 – 61

3

Helix

62 – 71

10

Beta strand

75 – 78

4

Beta strand

87 – 92

6

Helix

102 – 114

13

Beta strand

118 – 122

5

Beta strand

126 – 128

3

Helix

131 – 142

12

Beta strand

146 – 150

5

Turn

162 – 164

3

Beta strand

168 – 174

7

Beta strand

190 – 195

6

Beta strand

197 – 203

7

Turn

204 – 206

3

Beta strand

207 – 211

5

Helix

214 – 231

18

Helix

237 – 246

10

Helix

254 – 257

4

Helix

264 – 267

4

Sequences

	Sequence		Length	Mass (Da)
	P29600-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 4D89F8778999BF8D	FASTA	269	26,698
	10 20 30 40 50 60 AQSVPWGISR VQAPAAHNRG LTGSGVKVAV LDTGISTHPD LNIRGGASFV PGEPSTQDGN 70 80 90 100 110 120 GHGTHVAGTI AALNNSIGVL GVAPSAELYA VKVLGASGSG SVSSIAQGLE WAGNNGMHVA 130 140 150 160 170 180 NLSLGSPSPS ATLEQAVNSA TSRGVLVVAA SGNSGAGSIS YPARYANAMA VGATDQNNNR 190 200 210 220 230 240 ASFSQYGAGL DIVAPGVNVQ STYPGSTYAS LNGTSMATPH VAGAAALVKQ KNPSWSNVQI 250 260 RNHLKNTATS LGSTNLYGSG LVNAEAATR

References

[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: 1738156] [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: 8654411] [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: 9753430] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.78 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C9J	X-ray	1.80	A	1-267	[»]
1C9M	X-ray	1.67	A	1-269	[»]
1C9N	X-ray	1.50	A	1-267	[»]
1GCI	X-ray	0.78	A	1-269	[»]
1IAV	X-ray	1.80	A	1-269	[»]
1JEA	X-ray	2.00	A	1-269	[»]
1NDQ	X-ray	1.80	A	1-269	[»]
1NDU	X-ray	1.60	A	1-269	[»]
1Q5P	X-ray	1.60	A	1-269	[»]
1SVN	X-ray	1.40	A	1-269	[»]
1TK2	X-ray	1.54	A	1-263	[»]
3BX1	X-ray	1.85	A/B	1-269	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.4.21.62. 18569.

Family and domain databases

InterPro

IPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PRINTS

PR00723. SUBTILISIN.

PROSITE

PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SUBS_BACLE

Accession

Primary (citable) accession number: P29600

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)