Reviewed, UniProtKB/Swiss-Prot P00780 (SUBT_BACLI)

Names and origin

Protein names

Recommended name:
    Subtilisin Carlsberg
    EC=3.4.21.62

Gene names

Name:

apr

Organism

Bacillus licheniformis

Taxonomic identifier

1402 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 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.
Sequence similarities	Belongs to the peptidase S8 family.

Ontologies

Keywords
Biological process	Sporulation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of catalytic activity Inferred from electronic annotation. Source: InterPro 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 identical protein binding Inferred from electronic annotation. Source: InterPro 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

Signal peptide

1 – 29

29

Potential

Propeptide

30 – 105

76

Ref.2

PRO_0000027179

Chain

106 – 379

274

Subtilisin Carlsberg

PRO_0000027180

Sites

Active site

137

1

By similarity

Active site

168

1

By similarity

Active site

325

1

By similarity

Metal binding

107

1

Calcium 1

Metal binding

146

1

Calcium 1

Metal binding

179

1

Calcium 1; via carbonyl oxygen

Metal binding

181

1

Calcium 1

Metal binding

185

1

Calcium 1; via carbonyl oxygen

Metal binding

273

1

Calcium 2; via carbonyl oxygen

Metal binding

275

1

Calcium 2; via carbonyl oxygen

Metal binding

278

1

Calcium 2; via carbonyl oxygen

Experimental info

Sequence conflict

207

1

T → S AA sequence Ref.2

Sequence conflict

233

1

P → A AA sequence Ref.2

Sequence conflict

262 – 265

4

SSGN → NSGS AA sequence Ref.2

Sequence conflict

316

1

S → N AA sequence Ref.2

Secondary structure

1

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379

Helix Strand Turn

Details...

Helix

112 – 115

4

Helix

118 – 123

6

Beta strand

132 – 138

7

Beta strand

149 – 154

6

Beta strand

165 – 167

3

Helix

168 – 177

10

Beta strand

180 – 184

5

Beta strand

192 – 198

7

Beta strand

204 – 206

3

Helix

208 – 220

13

Beta strand

224 – 228

5

Beta strand

230 – 234

5

Helix

237 – 248

12

Beta strand

252 – 256

5

Turn

272 – 274

3

Beta strand

278 – 284

7

Beta strand

300 – 305

6

Beta strand

307 – 313

7

Turn

314 – 316

3

Beta strand

317 – 321

5

Helix

324 – 341

18

Helix

347 – 356

10

Helix

364 – 367

4

Helix

374 – 377

4

Sequences

	Sequence		Length	Mass (Da)
	P00780-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: F19A6DC5761FB504	FASTA	379	38,908
	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

References

[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: 3001653] [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: 4967581] [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: 8512925] [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: 9425066] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 106-379.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03341 Genomic DNA. Translation: CAB56500.1.

PIR

SUBSCL. A24111.

3D structure databases

PDBPDBe

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	106-379	[»]
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	[»]
3VSB	X-ray	2.60	A	106-379	[»]

ModBase

Search...

Protein family/group databases

MEROPS

I09.001.
S08.001.

Enzyme and pathway databases

BRENDA

3.4.21.62. 1017.

Family and domain databases

InterPro

IPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR010259. Prot_inh_S8A.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF05922. Inhibitor_I9. 1 hit.
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

SUBT_BACLI

Accession

Primary (citable) accession number: P00780

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 88 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)