Reviewed, UniProtKB/Swiss-Prot P00783 (SUBT_BACSA)

Names and origin

Protein names

Recommended name:
    Subtilisin amylosacchariticus
    EC=3.4.21.62

Gene names

Name:

apr

Organism

Bacillus subtilis subsp. amylosacchariticus

Taxonomic identifier

1483 [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 By similarity.
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	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 – 30	30	Potential
	Propeptide	31 – 106	76	Potential		PRO_0000027183
	Chain	107 – 381	275	Subtilisin amylosacchariticus		PRO_0000027184
Sites
	Active site	138	1	Charge relay system By similarity
	Active site	170	1	Charge relay system By similarity
	Active site	327	1	Charge relay system By similarity
	Metal binding	108	1	Calcium 1 By similarity
	Metal binding	147	1	Calcium 1 By similarity
	Metal binding	181	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	183	1	Calcium 1 By similarity
	Metal binding	185	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	187	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	275	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	277	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	280	1	Calcium 2; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	191	1	S → A AA sequence Ref.2
	Sequence conflict	365	1	N → D AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00783-1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: 2251BADE22B4824F	FASTA	381	39,467
	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 SPSASLYAVK VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPSGSTA 250 260 270 280 290 300 LKTVVDKAVS SGIVVAAAAG NEGSSGSSST VGYPAKYPST IAVGAVNSSN QRASFSSAGS 310 320 330 340 350 360 ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTA 370 380 TYLGNSFYYG KGLINVQAAA Q

References

[1]	"Cloning and expression of subtilisin amylosacchariticus gene." Yoshimoto T., Oyama H., Honda T., Tone H., Takeshita T., Kamiyama T., Tsuru D. J. Biochem. 103:1060-1065(1988) [PubMed: 3139650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Subtilisin Amylosacchariticus. II. Isolation and sequence of the tryptic and cyanogen bromide peptides." Markland F.S., Kurihara M., Smith E.L. J. Biol. Chem. 247:5602-5618(1972) [PubMed: 4560201] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[3]	"Subtilisin Amylosacchariticus. 3. Isolation and sequence of the chymotryptic peptides and the complete amino acid sequence." Kurihara M., Markland F.S., Smith E.L. J. Biol. Chem. 247:5619-5631(1972) [PubMed: 5055784] [Abstract] Cited for: PROTEIN SEQUENCE OF 107-381.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00264 Genomic DNA. Translation: BAA00186.1.
PIR	SUBSS. A41448.
3D structure databases
HSSP	HSSP built from PDB template 1SCJ based on UniProtKB P04189.
SMR	P00783. Positions 36-106, 107-381.
ModBase	Search...
Protein family/group databases
MEROPS	I09.001. S08.042.
Enzyme and pathway databases
BRENDA	3.4.21.62. 289877.
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_BACSA

Accession

Primary (citable) accession number: P00783

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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