Reviewed, UniProtKB/Swiss-Prot P00777 (PRTB_STRGR)

Names and origin

Protein names

Recommended name:
    Streptogrisin-B
    EC=3.4.21.81
Alternative name(s):
    Serine protease B
    SGPB
    Pronase enzyme B

Gene names

Name:

sprB

Organism

Streptomyces griseus

Taxonomic identifier

1911 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	299 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	Has a primary specificity for large aliphatic or aromatic amino acids.
Catalytic activity	Hydrolysis of proteins with trypsin-like specificity.
Subunit structure	Monomer.
Sequence similarities	Belongs to the peptidase S1 family.

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: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
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 – 38

38

Propeptide

39 – 114

76

Ref.2

PRO_0000026911

Chain

115 – 299

185

Streptogrisin-B

PRO_0000026912

Sites

Active site

147

1

Charge relay system Ref.6 Ref.7

Active site

177

1

Charge relay system Ref.6 Ref.7

Active site

255

1

Charge relay system Ref.6 Ref.7

Amino acid modifications

Disulfide bond

128 ↔ 148

Disulfide bond

249 ↔ 276

Experimental info

Sequence conflict

153

1

T → TG AA sequence Ref.2

Sequence conflict

157

1

Missing AA sequence Ref.2

Sequence conflict

293

1

A → V AA sequence Ref.2

Sequence conflict

296

1

V → A AA sequence Ref.2

Secondary structure

1

.

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299

Helix Strand Turn

Details...

Beta strand

120 – 122

3

Beta strand

127 – 129

3

Beta strand

132 – 136

5

Beta strand

139 – 144

6

Helix

146 – 149

4

Beta strand

153 – 158

6

Beta strand

163 – 172

10

Beta strand

174 – 176

3

Beta strand

178 – 183

6

Beta strand

186 – 188

3

Beta strand

210 – 215

6

Turn

216 – 218

3

Beta strand

219 – 233

15

Beta strand

239 – 247

9

Beta strand

258 – 261

4

Beta strand

264 – 275

12

Turn

276 – 278

3

Beta strand

279 – 286

8

Helix

287 – 294

8

Sequences

	Sequence		Length	Mass (Da)
	P00777-1 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 7A272C9516C7B9B1	FASTA	299	30,554
	10 20 30 40 50 60 MRIKRTSNRS NAARRVRTTA VLAGLAAVAA LAVPTANAET PRTFSANQLT AASDAVLGAD 70 80 90 100 110 120 IAGTAWNIDP QSKRLVVTVD STVSKAEINQ IKKSAGANAD ALRIERTPGK FTKLISGGDA 130 140 150 160 170 180 IYSSTGRCSL GFNVRSGSTY YFLTAGHCTD GATTWWANSA RTTVLGTTSG SSFPNNDYGI 190 200 210 220 230 240 VRYTNTTIPK DGTVGGQDIT SAANATVGMA VTRRGSTTGT HSGSVTALNA TVNYGGGDVV 250 260 270 280 290 YGMIRTNVCA EPGDSGGPLY SGTRAIGLTS GGSGNCSSGG TTFFQPVTEA LSAYGVSVY

References

[1]	"Characterization and structure of genes for proteases A and B from Streptomyces griseus." Henderson G., Krygsman P., Liu C.J., Davey C.C., Malek L.T. J. Bacteriol. 169:3778-3784(1987) [PubMed: 3112129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT OF Pronase." Jurasek L., Carpenter M.R., Smillie L.B., Gertler A., Levy S., Ericsson L.H. Biochem. Biophys. Res. Commun. 61:1095-1100(1974) [PubMed: 4218101] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-299. Strain: K-1.
[3]	"Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes." Delbaere L.T.J., Hutcheon W.L.B., James M.N.G., Thiessen W.E. Nature 257:758-763(1975) [PubMed: 1186854] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[4]	"The 2.8-A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A." Delbaere L.T.J., Brayer G.D., James M.N.G. Can. J. Biochem. 57:135-144(1979) [PubMed: 110426] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[5]	"Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1-A resolution." Greenblatt H.M., Ryan C.A., James M.N.G. J. Mol. Biol. 205:201-228(1989) [PubMed: 2494344] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]	"Inhibition of Streptomyces griseus protease B by peptide chloromethyl ketones: partial mapping of the binding site and identification of the reactive residue." Gertler A. FEBS Lett. 43:81-85(1974) [PubMed: 4212092] [Abstract] Cited for: ACTIVE SITE.
[7]	"Studies on Streptomyces griseus protease. II. The amino acid sequence around the reactive serine residue of DFP-sensitive components with esterase activity." Wahlby S., Engstrom L. Biochim. Biophys. Acta 151:402-408(1968) [PubMed: 5636372] [Abstract] Cited for: ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M17104 Genomic DNA. Translation: AAA26819.1.

PIR

PRSMBG. B26974.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CSO	X-ray	1.90	E	115-299	[»]
1CT0	X-ray	1.80	E	115-299	[»]
1CT2	X-ray	1.65	E	115-299	[»]
1CT4	X-ray	1.60	E	115-299	[»]
1DS2	X-ray	1.70	E	115-299	[»]
1SGD	X-ray	1.80	E	115-299	[»]
1SGE	X-ray	1.80	E	115-299	[»]
1SGN	X-ray	1.80	E	115-299	[»]
1SGP	X-ray	1.40	E	115-299	[»]
1SGQ	X-ray	1.90	E	115-299	[»]
1SGR	X-ray	1.80	E	115-299	[»]
1SGY	X-ray	1.80	E	115-299	[»]
2GKV	X-ray	1.70	E	115-299	[»]
2NU0	X-ray	1.95	E	115-299	[»]
2NU1	X-ray	1.80	E	115-299	[»]
2NU2	X-ray	1.65	E	115-299	[»]
2NU3	X-ray	1.80	E	115-299	[»]
2NU4	X-ray	1.75	E	115-299	[»]
2QA9	X-ray	1.18	E	115-299	[»]
			I	119-122	[»]
2QAA	X-ray	1.23	A/B	115-299	[»]
2SGD	X-ray	1.80	E	115-299	[»]
2SGE	X-ray	1.80	E	115-299	[»]
2SGF	X-ray	1.75	E	115-299	[»]
2SGP	X-ray	1.80	E	115-299	[»]
2SGQ	X-ray	1.80	E	115-299	[»]
3SGB	X-ray	1.80	E	115-299	[»]
3SGQ	X-ray	1.80	E	115-299	[»]
4SGB	X-ray	2.10	E	115-299	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.262.

Enzyme and pathway databases

BRENDA

3.4.21.81. 1270.

Family and domain databases

InterPro

IPR004236. Pept_S1_alpha_lytic.
IPR001316. Pept_S1A_streptogrisin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
[Graphical view]

Pfam

PF02983. Pro_Al_protease. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001134. Streptogrisin. 1 hit.

PRINTS

PR00861. ALYTICPTASE.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

PMAP-CutDB

P00777.

Entry information

Entry name

PRTB_STRGR

Accession

Primary (citable) accession number: P00777

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 84 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)