P08594 (AQL1_THEAQ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aqualysin-1
EC=3.4.21.111

Alternative name(s):
Aqualysin-I

Gene names

Name:

pstI

Organism

Thermus aquaticus

Taxonomic identifier

271 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	513 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	Aqualysin I is a thermophilic alkaline serine protease.
Catalytic activity	Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.
Subcellular location	Secreted.
Developmental stage	Secreted from the early stationary phase until the time the cells cease to grow.
Post-translational modification	The N- and C-terminal Pro-sequences are successively removed through the proteolytic activity of PstI itself. The C-terminal Pro-sequence is required for translocation of the proteases across the outer membrane.
Sequence similarities	Belongs to the peptidase S8 family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 80 degrees Celsius for caseinolytic activity.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Autocatalytic cleavage Disulfide bond Zymogen
Technical term	3D-structure 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: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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 – 14

14

Ref.1

Propeptide

15 – 127

113

PRO_0000026992

Chain

128 – 408

281

Aqualysin-1

PRO_0000026993

Propeptide

409 – 513

105

PRO_0000026994

Sites

Active site

166

1

Charge relay system By similarity

Active site

197

1

Charge relay system By similarity

Active site

349

1

Charge relay system By similarity

Amino acid modifications

Disulfide bond

194 ↔ 226

Ref.4

Disulfide bond

290 ↔ 321

Ref.4

Secondary structure

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513

Helix Strand Turn

Details...

Beta strand

129 – 132

4

Helix

135 – 140

6

Beta strand

142 – 146

5

Beta strand

161 – 167

7

Helix

174 – 176

3

Beta strand

180 – 185

6

Beta strand

194 – 196

3

Helix

197 – 206

10

Turn

208 – 210

3

Beta strand

217 – 222

6

Helix

232 – 245

14

Beta strand

248 – 254

7

Helix

262 – 273

12

Beta strand

277 – 281

5

Beta strand

284 – 288

5

Helix

289 – 291

3

Turn

294 – 296

3

Beta strand

300 – 306

7

Beta strand

310 – 312

3

Beta strand

324 – 327

4

Beta strand

329 – 334

6

Beta strand

338 – 340

3

Beta strand

342 – 345

4

Helix

348 – 365

18

Helix

371 – 381

11

Beta strand

382 – 385

4

Sequences

	Sequence		Length	Mass (Da)
	P08594 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: DDFDFE6D4A50B785	FASTA	513	53,913
	10 20 30 40 50 60 MRKTYWLMAL FAVLVLGGCQ MASRSDPTPT LAEAFWPKEA PVYGLDDPEA IPGRYIVVFK 70 80 90 100 110 120 KGKGQSLLQG GITTLQARLA PQGVVVTQAY TGALQGFAAE MAPQALEAFR QSPDVEFIEA 130 140 150 160 170 180 DKVVRAWATQ SPAPWGLDRI DQRDLPLSNS YTYTATGRGV NVYVIDTGIR TTHREFGGRA 190 200 210 220 230 240 RVGYDALGGN GQDCNGHGTH VAGTIGGVTY GVAKAVNLYA VRVLDCNGSG STSGVIAGVD 250 260 270 280 290 300 WVTRNHRRPA VANMSLGGGV STALDNAVKN SIAAGVVYAV AAGNDNANAC NYSPARVAEA 310 320 330 340 350 360 LTVGATTSSD ARASFSNYGS CVDLFAPGAS IPSAWYTSDT ATQTLNGTSM ATPHVAGVAA 370 380 390 400 410 420 LYLEQNPSAT PASVASAILN GATTGRLSGI GSGSPNRLLY SLLSSGSGST APCTSCSYYT 430 440 450 460 470 480 GSLSGPGDYN FQPNGTYYYS PAGTHRAWLR GPAGTDFDLY LWRWDGSRWL TVGSSTGPTS 490 500 510 EESLSYSGTA GYYLWRIYAY SGSGMYEFWL QRP

References

[1]	"Unique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli." Terada I., Kwon S.-T., Miyata Y., Matsuzawa H., Ohta T. J. Biol. Chem. 265:6576-6581(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-23. Strain: YT1.
[2]	"Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme." Kwon S.-T., Terada I., Matsuzawa H., Ohta T. Eur. J. Biochem. 173:491-497(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-442, PARTIAL PROTEIN SEQUENCE. Strain: YT1.
[3]	"Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1." Matsuzawa H., Tokugawa K., Hamaoki M., Mizoguchi M., Taguchi H., Terada I., Kwon S.-T., Ohta T. Eur. J. Biochem. 171:441-447(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 128-170.
[4]	"Role of disulphide bonds in a thermophilic serine protease aqualysin I from Thermus aquaticus YT-1." Sakaguchi M., Takezawa M., Nakazawa R., Nozawa K., Kusakawa T., Nagasawa T., Sugahara Y., Kawakita M. J. Biochem. 143:625-632(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D90108 Genomic DNA. Translation: BAA14135.1.
X07734 Genomic DNA. Translation: CAA30559.1.

PIR

A35742.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DZT	X-ray	1.95	A	128-403	[»]

ProteinModelPortal

P08594.

SMR

P08594. Positions 128-402.

ModBase

Search...

Protein family/group databases

MEROPS

S08.051.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12998.

Family and domain databases

Gene3D

3.40.50.200. 1 hit.

InterPro

IPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]

PANTHER

PTHR10795. PTHR10795. 1 hit.

Pfam

PF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PRINTS

PR00723. SUBTILISIN.

SUPFAM

SSF52743. Pept_S8_S53. 1 hit.
SSF54897. Prot_inh_propept. 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

AQL1_THEAQ

Accession

Primary (citable) accession number: P08594

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program