Reviewed, UniProtKB/Swiss-Prot P07518 (SUBT_BACPU)

Names and origin

Protein names

Recommended name:
    Subtilisin
    EC=3.4.21.62
Alternative name(s):
    Alkaline mesentericopeptidase

Gene names

Name:

apr

Organism

Bacillus pumilus (Bacillus mesentericus)

Taxonomic identifier

1408 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	275 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.
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 Direct protein sequencing
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 – 275

275

Subtilisin

PRO_0000076419

Sites

Active site

32

1

By similarity

Active site

64

1

By similarity

Active site

221

1

By similarity

Metal binding

2

1

Calcium 1

Metal binding

41

1

Calcium 1

Metal binding

75

1

Calcium 1; via carbonyl oxygen

Metal binding

77

1

Calcium 1

Metal binding

79

1

Calcium 1; via carbonyl oxygen

Metal binding

81

1

Calcium 1; via carbonyl oxygen

Metal binding

169

1

Calcium 2; via carbonyl oxygen

Metal binding

171

1

Calcium 2; via carbonyl oxygen

Metal binding

174

1

Calcium 2; via carbonyl oxygen

Secondary structure

1

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275

Helix Strand Turn

Details...

Helix

6 – 10

5

Helix

13 – 19

7

Beta strand

27 – 33

7

Beta strand

44 – 49

6

Helix

65 – 73

9

Beta strand

76 – 80

5

Beta strand

88 – 94

7

Helix

104 – 116

13

Beta strand

120 – 124

5

Beta strand

126 – 130

5

Helix

133 – 144

12

Beta strand

148 – 152

5

Turn

168 – 170

3

Beta strand

174 – 180

7

Beta strand

198 – 201

4

Beta strand

203 – 209

7

Turn

210 – 212

3

Beta strand

213 – 217

5

Helix

220 – 237

18

Helix

243 – 252

10

Helix

260 – 263

4

Helix

270 – 273

4

Sequences

	Sequence		Length	Mass (Da)
	P07518-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 33BDA897DBA4170A	FASTA	275	27,656
	10 20 30 40 50 60 AQSVPYGISQ IKAPALHSQG YTGSNVKVAV IDSGIDSSHP DLNVRGGASF VPSETNPYQD 70 80 90 100 110 120 GSSHGTHVAG TIAALNNSIG VLGVAPSSAL YAVKVLDSTG SGQYSWIING IEWAISNNMD 130 140 150 160 170 180 VINMSLGGPT GSTALKTVVD KAVSSGIVVA AAAGNEGSSG STSTVGYPAK YPSTIAVGAV 190 200 210 220 230 240 NSANQRASFS SAGSELDVMA PGVSIQSTLP GGTYGAYNGT SMATPHVAGA AALILSKHPT 250 260 270 WTNAQVRDRL ESTATYLGSS FYYGKGLINV QAAAQ

References

[1]	"Complete amino acid sequence of alkaline mesentericopeptidase: a subtilisin isolated from a strain of Bacillus mesentericus." Svendsen I., Genov N., Idakieva K. FEBS Lett. 196:228-232(1986) Cited for: PROTEIN SEQUENCE.
[2]	"Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C." Dauter Z., Betzel C., Genov N., Pipon N., Wilson K.S. Acta Crystallogr. B 47:707-730(1991) [PubMed: 1793542] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

PIR

A23624.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MEE	X-ray	2.00	A	1-275	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S08.002.

Enzyme and pathway databases

BRENDA

3.4.21.62. 1189.

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

SUBT_BACPU

Accession

Primary (citable) accession number: P07518

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
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)