Reviewed, UniProtKB/Swiss-Prot P04189 (SUBT_BACSU)

Names and origin

Protein names

Recommended name:
    Subtilisin E
    EC=3.4.21.62

Gene names

Name:	aprE
Synonyms:	apr, aprA, sprE
Ordered Locus Names:	BSU10300

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	381 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.
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 Complete proteome
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 – 23

23

Potential

Propeptide

24 – 106

83

Potential

PRO_0000027187

Chain

107 – 381

275

Subtilisin E

PRO_0000027188

Sites

Active site

138

1

Charge relay system

Active site

170

1

Charge relay system

Active site

327

1

Charge relay system

Metal binding

108

1

Calcium 1

Metal binding

147

1

Calcium 1

Metal binding

181

1

Calcium 1; via carbonyl oxygen

Metal binding

183

1

Calcium 1

Metal binding

185

1

Calcium 1; via carbonyl oxygen

Metal binding

187

1

Calcium 1; via carbonyl oxygen

Metal binding

275

1

Calcium 2; via carbonyl oxygen

Metal binding

277

1

Calcium 2; via carbonyl oxygen

Metal binding

280

1

Calcium 2; via carbonyl oxygen

Experimental info

Sequence conflict

27

1

A → V in CAA74536. Ref.2

Sequence conflict

191

1

A → S in AAA22742. Ref.1

Sequence conflict

191

1

A → S in CAA74536. Ref.2

Sequence conflict

191

1

A → S Ref.7

Secondary structure

1

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381

Helix Strand Turn

Details...

Beta strand

37 – 43

7

Beta strand

45 – 48

4

Helix

52 – 60

9

Turn

61 – 63

3

Beta strand

65 – 69

5

Beta strand

71 – 80

10

Helix

82 – 89

8

Beta strand

94 – 99

6

Beta strand

102 – 105

4

Helix

112 – 116

5

Helix

119 – 125

7

Beta strand

133 – 139

7

Beta strand

150 – 155

6

Beta strand

167 – 169

3

Helix

170 – 179

10

Beta strand

183 – 186

4

Beta strand

195 – 200

6

Beta strand

206 – 209

4

Helix

210 – 222

13

Beta strand

226 – 230

5

Beta strand

232 – 235

4

Helix

239 – 250

12

Beta strand

254 – 258

5

Turn

274 – 276

3

Beta strand

280 – 286

7

Beta strand

304 – 307

4

Beta strand

309 – 315

7

Turn

316 – 318

3

Beta strand

319 – 323

5

Helix

326 – 343

18

Helix

349 – 358

10

Helix

366 – 369

4

Helix

376 – 379

4

Sequences

	Sequence		Length	Mass (Da)
	P04189-1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 5C8A4B0E42FCE83D	FASTA	381	39,479
	10 20 30 40 50 60 MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM SSAKKKDVIS 70 80 90 100 110 120 EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED HIAHEYAQSV PYGISQIKAP 130 140 150 160 170 180 ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV RGGASFVPSE TNPYQDGSSH GTHVAGTIAA 190 200 210 220 230 240 LNNSIGVLGV APSASLYAVK VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPTGSTA 250 260 270 280 290 300 LKTVVDKAVS SGIVVAAAAG NEGSSGSTST VGYPAKYPST IAVGAVNSSN QRASFSSAGS 310 320 330 340 350 360 ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTA 370 380 TYLGNSFYYG KGLINVQAAA Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Replacement of the Bacillus subtilis subtilisin structural gene with an In vitro-derived deletion mutation." Stahl M.L., Ferrari E. J. Bacteriol. 158:411-418(1984) [PubMed: 6427178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene." Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S. Microbiology 144:859-875(1998) [PubMed: 9579061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 0:0-0(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 27 AND 191.
[5]	"The subtilisin E gene of Bacillus subtilis is transcribed from a sigma 37 promoter in vivo." Wong S.L., Price C.W., Goldfarb D.S., Doi R.H. Proc. Natl. Acad. Sci. U.S.A. 81:1184-1188(1984) [PubMed: 6322190] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156. Strain: 168 / PY79.
[6]	"Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli." Ikemura H., Takagi H., Inouye M. J. Biol. Chem. 262:7859-7864(1987) [PubMed: 3108260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156. Strain: 168 / PY79.
[7]	"Isolation, characterization and structure of subtilisin from a thermostable Bacillus subtilis isolate." Kamal M., Hoeoeg J.-O., Kaiser R., Shafqat J., Razzaki T., Zaidi Z.H., Joernvall H. FEBS Lett. 374:363-366(1995) [PubMed: 7589571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-323. Strain: RT-5.
[8]	"Bacillus subtilis subtilisin gene (aprE) is expressed from a sigma A (sigma 43) promoter in vitro and in vivo." Park S.S., Wong S.L., Wang L.F., Doi R.H. J. Bacteriol. 171:2657-2665(1989) [PubMed: 2496113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. Strain: 168.
[9]	"Location of the targets of the hpr-97, sacU32(Hy), and sacQ36(Hy) mutations in upstream regions of the subtilisin promoter." Henner D.J., Ferrari E., Perego M., Hoch J.A. J. Bacteriol. 170:296-300(1988) [PubMed: 2447063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[10]	"The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0-A resolution." Jain S.C., Shinde U., Li Y., Inouye M., Berman H.M. J. Mol. Biol. 284:137-144(1998) [PubMed: 9811547] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Strain: 168.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K01988 Genomic DNA. Translation: AAA22742.1.
Y14083 Genomic DNA. Translation: CAA74536.1.
AL009126 Genomic DNA. Translation: CAB12870.2.
K01443 Genomic DNA. Translation: AAA22814.1.
M16639 Genomic DNA. Translation: AAA22744.1.
M31060 Genomic DNA. Translation: AAA22246.1.
M19125 Genomic DNA. Translation: AAA22245.1.

PIR

SUBSI. A00972.

RefSeq

NP_388911.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SCJ	X-ray	2.00	A	107-381	[»]
			B	36-106	[»]

DisProt

DP00394.

ModBase

Search...

Protein family/group databases

MEROPS

I09.001.

Genome annotation databases

GeneID

939313.

GenomeReviews

Gene locus BSU10300 in contig AL009126_GR.

KEGG

bsu:BSU10300.

NMPDR

fig|224308.1.peg.1030.

Organism-specific databases

SubtiList

BG10190. aprE. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P04189.

OMA

P04189. MDVINMS.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU1030-MON.

BRENDA

3.4.21.62. 150.

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_BACSU

Accession

Primary (citable) accession number: P04189
Secondary accession number(s): O07613, P70989

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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