P00775 (TRYP_STRGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trypsin
EC=3.4.21.4

Alternative name(s):
SGT

Gene names

Name:

sprT

Organism

Streptomyces griseus

Taxonomic identifier

1911 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces griseus group

Protein attributes

Sequence length	259 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)

Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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 – 32

32

Propeptide

33 – 36

4

Activation peptide

PRO_0000028307

Chain

37 – 259

223

Trypsin

PRO_0000028308

Regions

Domain

37 – 257

221

Peptidase S1

Sites

Active site

73

1

Charge relay system

Active site

118

1

Charge relay system

Active site

208

1

Charge relay system

Site

202

1

Required for specificity

Amino acid modifications

Disulfide bond

58 ↔ 74

Disulfide bond

177 ↔ 192

Disulfide bond

204 ↔ 233

Experimental info

Sequence conflict

95 – 96

2

Missing AA sequence Ref.2

Secondary structure

1

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259

Helix Strand Turn

Details...

Turn

45 – 47

3

Beta strand

51 – 54

4

Turn

55 – 57

3

Beta strand

58 – 64

7

Beta strand

67 – 70

4

Helix

72 – 74

3

Beta strand

77 – 81

5

Beta strand

85 – 89

5

Beta strand

91 – 95

5

Beta strand

99 – 108

10

Helix

113 – 115

3

Beta strand

120 – 126

7

Beta strand

137 – 139

3

Beta strand

142 – 152

11

Beta strand

165 – 172

8

Helix

174 – 180

7

Helix

182 – 184

3

Helix

187 – 189

3

Beta strand

190 – 193

4

Beta strand

197 – 200

4

Beta strand

211 – 215

5

Beta strand

221 – 234

14

Beta strand

240 – 244

5

Helix

245 – 256

12

Sequences

	Sequence		Length	Mass (Da)
	P00775 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 050233AFF1F64823	FASTA	259	26,776
	10 20 30 40 50 60 MKHFLRALKR CSVAVATVAI AVVGLQPVTA SAAPNPVVGG TRAAQGEFPF MVRLSMGCGG 70 80 90 100 110 120 ALYAQDIVLT AAHCVSGSGN NTSITATGGV VDLQSSSAVK VRSTKVLQAP GYNGTGKDWA 130 140 150 160 170 180 LIKLAQPINQ PTLKIATTTA YNQGTFTVAG WGANREGGSQ QRYLLKANVP FVSDAACRSA 190 200 210 220 230 240 YGNELVANEE ICAGYPDTGG VDTCQGDSGG PMFRKDNADE WIQVGIVSWG YGCARPGYPG 250 VYTEVSTFAS AIASAARTL

References

[1]	"Molecular cloning and nucleotide sequence of Streptomyces griseus trypsin gene." Kim J.C., Cha S.H., Jeong S.T., Oh S.K., Byun S.M. Biochem. Biophys. Res. Commun. 181:707-713(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10137 / DSM 40855 / NBRC 3430 / NCIMB 8232 / NCTC 6961.
[2]	"Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence." Olafson R.W., Jurasek L., Carpenter M.R., Smillie L.B. Biochemistry 14:1168-1177(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 37-259.
[3]	"Refined crystal structure of Streptomyces griseus trypsin at 1.7-A resolution." Read R.J., James M.N.G. J. Mol. Biol. 200:523-551(1988) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64471 Genomic DNA. Translation: AAA26820.1. Sequence problems.

PIR

TRSMG. JQ1302.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OS8	X-ray	1.55	A	37-259	[»]
1OSS	X-ray	1.93	A	37-259	[»]
1SGT	X-ray	1.70	A	37-259	[»]
2FMJ	X-ray	1.65	A	37-251	[»]
3BEU	X-ray	1.05	A/B	37-259	[»]
3I77	X-ray	2.10	A	37-259	[»]
3I78	X-ray	3.00	A	37-259	[»]

ProteinModelPortal

P00775.

SMR

P00775. Positions 37-259.

ModBase

Search...

Protein family/group databases

MEROPS

S01.101.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.4.21.4. 6035.

Family and domain databases

InterPro

IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00775.

Entry information

Entry name

TRYP_STRGR

Accession

Primary (citable) accession number: P00775

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program