P29599 (SUBB_BACLE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Subtilisin BL 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.
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
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW 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	metal 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 BL

PRO_0000076416

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

86 – 92

7

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

178 – 180

3

Beta strand

192 – 195

4

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)
	P29599 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: E8AFF1A6A9E2676B	FASTA	269	26,824
	10 20 30 40 50 60 AQSVPWGISR VQAPAAHNRG LTGSGVKVAV LDTGISTHPD LNIRGGASFV PGEPSTQDGN 70 80 90 100 110 120 GHGTHVAGTI AALNNSIGVL GVAPSAELYA VKVLGADGRG AISSIAQGLE WAGNNGMHVA 130 140 150 160 170 180 NLSLGSPSPS ATLEQAVNSA TSRGVLVVAA SGNSGASSIS YPARYANAMA VGATDQNNNR 190 200 210 220 230 240 ASFSQYGAGL DIVAPGVNVQ STYPGSTYAS LNGTSMATPH VAGAAALVKQ KNPSWSNVQI 250 260 RNHLKNTATS LGSTNLYGSG LVNAEAATR

References

[1]	"The crystal structure of the Bacillus lentus alkaline protease, subtilisin BL, at 1.4-A resolution." Goddette D.W., Paech C., Yang S.S., Mielenz J.R., Bystroff C., Wilke M.E., Fletterick R.J. J. Mol. Biol. 228:580-595(1992) [PubMed: 1453465] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ST3	X-ray	1.40	A	2-269	[»]

ProteinModelPortal

P29599.

SMR

P29599. Positions 1-269.

ModBase

Search...

Protein family/group databases

MEROPS

S08.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000209. Peptidase_S8/S53.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
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.

SUPFAM

SSF52743. Pept_S8_S53. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

SUBB_BACLE

Accession

Primary (citable) accession number: P29599

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program