Reviewed, UniProtKB/Swiss-Prot P00781 (SUBD_BACLI)

Names and origin

Protein names

Recommended name:
    Subtilisin DY
    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	274 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 – 274

274

Subtilisin DY

PRO_0000076417

Sites

Active site

32

1

Charge relay system

Active site

63

1

Charge relay system

Active site

220

1

Charge relay system

Metal binding

2

1

Calcium 1

Metal binding

41

1

Calcium 1

Metal binding

74

1

Calcium 1; via carbonyl oxygen

Metal binding

76

1

Calcium 1

Metal binding

80

1

Calcium 1; via carbonyl oxygen

Metal binding

168

1

Calcium 2; via carbonyl oxygen

Metal binding

170

1

Calcium 2; via carbonyl oxygen

Metal binding

173

1

Calcium 2; via carbonyl oxygen

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

274

Helix Strand Turn

Details...

Helix

7 – 10

4

Helix

13 – 18

6

Beta strand

27 – 33

7

Beta strand

44 – 49

6

Beta strand

60 – 62

3

Helix

63 – 72

10

Beta strand

75 – 79

5

Beta strand

87 – 93

7

Helix

103 – 115

13

Beta strand

119 – 123

5

Helix

132 – 143

12

Beta strand

147 – 151

5

Turn

167 – 169

3

Beta strand

173 – 179

7

Beta strand

195 – 200

6

Beta strand

202 – 208

7

Turn

209 – 211

3

Beta strand

212 – 216

5

Helix

219 – 236

18

Helix

242 – 251

10

Helix

259 – 262

4

Helix

269 – 272

4

Sequences

	Sequence		Length	Mass (Da)
	P00781-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0154696E22F46533	FASTA	274	27,436
	10 20 30 40 50 60 AQTVPYGIPL IKADKVQAQG YKGANVKVGI IDTGIAASHT DLKVVGGASF VSGESYNTDG 70 80 90 100 110 120 NGHGTHVAGT VAALDNTTGV LGVAPNVSLY AIKVLNSSGS GTYSAIVSGI EWATQNGLDV 130 140 150 160 170 180 INMSLGGPSG STALKQAVDK AYASGIVVVA AAGNSGSSGS QNTIGYPAKY DSVIAVGAVD 190 200 210 220 230 240 SNKNRASFSS VGAELEVMAP GVSVYSTYPS NTYTSLNGTS MASPHVAGAA ALILSKYPTL 250 260 270 SASQVRNRLS STATNLGDSF YYGKGLINVE AAAQ

References

[1]	"Primary structure of subtilisin DY." Nedkov P., Oberthur W., Braunitzer G. Hoppe-Seyler's Z. Physiol. Chem. 364:1537-1540(1983) [PubMed: 6420308] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: DY.
[2]	"Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg." Eschenburg S., Genov N., Peters K., Fittkau S., Stoeva S., Wilson K.S., Betzel C. Eur. J. Biochem. 257:309-318(1998) [PubMed: 9826175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). Strain: DY.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BH6	X-ray	1.75	A	1-274	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S08.037.

Enzyme and pathway databases

BRENDA

3.4.21.62. 1017.

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

SUBD_BACLI

Accession

Primary (citable) accession number: P00781

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 69 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)