[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3112129 [NCBI, ExPASy, EBI, Israel, Japan] Henderson G., Krygsman P., Liu C.J., Davey C.C., Malek L.T.; "Characterization and structure of genes for proteases A and B from Streptomyces griseus."; J. Bacteriol. 169:3778-3784(1987).
[2]	PROTEIN SEQUENCE OF 116-297. DOI=10.1016/0014-5793(74)80412-6; PubMed=4214713 [NCBI, ExPASy, EBI, Israel, Japan] Johnson P., Smillie L.B.; "The amino acid sequence and predicted structure of Streptomyces griseus protease A."; FEBS Lett. 47:1-6(1974).
[3]	SEQUENCE REVISION TO 249. Apostol I., Smillie L.B., Laskowski M. Jr.; Submitted (JUL-1996) to UniProtKB.
[4]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). DOI=10.1016/0022-2836(79)90486-8; PubMed=119870 [NCBI, ExPASy, EBI, Israel, Japan] Sielecki A.R., Hendrickson W.A., Broughton C.G., Delbaere L.T.J., Brayer G.D., James M.N.G.; "Protein structure refinement: Streptomyces griseus serine protease A at 1.8-A resolution."; J. Mol. Biol. 134:781-804(1979).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1016/0022-2836(78)90159-6; PubMed=101674 [NCBI, ExPASy, EBI, Israel, Japan] Brayer G.D., Delbaere L.T.J., James M.N.G.; "Molecular structure of crystalline Streptomyces griseus protease A at 2.8-A resolution. II. Molecular conformation, comparison with alpha-chymotrypsin and active-site geometry."; J. Mol. Biol. 124:261-283(1978).

Comments

FUNCTION: Has a primary specificity for large aliphatic or aromatic amino acids.
CATALYTIC ACTIVITY: Hydrolysis of proteins with specificity similar to chymotrypsin.
SUBUNIT: Monomer.
SIMILARITY: Belongs to the peptidase S1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M17103; AAA26818.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26974; PRSMAG.

3D structure databases

PDB

1SGC; X-ray; 1.80 A; A=117-297.	[ExPASy / RCSB / EBI]
2SGA; X-ray; 1.50 A; A=117-297.	[ExPASy / RCSB / EBI]
3SGA; X-ray; 1.80 A; E=117-297.	[ExPASy / RCSB / EBI]
4SGA; X-ray; 1.80 A; E=117-297.	[ExPASy / RCSB / EBI]
5SGA; X-ray; 1.80 A; E=117-297.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1SGC; -.
2SGA; -.
3SGA; -.
4SGA; -.
5SGA; -.

ModBase

P00776.

Protein family/group databases

MEROPS

S01.261; -.

Family and domain databases

InterPro

IPR004236; Pept_S1_alpha_lytic.
IPR001316; Pept_S1A_streptogrisin.
IPR001254; Peptidase_S1_S6.
Graphical view of domain structure.

Pfam

PF02983; Pro_Al_protease; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001134; Streptogrisin; 1.

PRINTS

PR00861; ALYTICPTASE.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.

Other

P00776; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; Protease; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 38`	`38`
`PROPEP`	`39 115`	`77`		`PRO_0000026909`
`CHAIN`	`116 297`	`182`	`Streptogrisin-A.`	`PRO_0000026910`
`ACT_SITE`	`149 149`		`Charge relay system (By similarity).`
`ACT_SITE`	`171 171`		`Charge relay system (By similarity).`
`ACT_SITE`	`253 253`		`Charge relay system (By similarity).`
`DISULFID`	`130 150`
`DISULFID`	`247 274`
`CONFLICT`	`151 151`		`T -> TS (in Ref. 2; AA sequence).`
`CONFLICT`	`184 184`		`D -> N (in Ref. 2; AA sequence).`
`STRAND`	`122 125`	`4`
`STRAND`	`128 131`	`4`
`STRAND`	`134 138`	`5`
`STRAND`	`141 146`	`6`
`HELIX`	`148 151`	`4`
`STRAND`	`155 157`	`3`
`STRAND`	`160 170`	`11`
`STRAND`	`172 178`	`7`
`HELIX`	`180 182`	`3`
`STRAND`	`186 188`	`3`
`STRAND`	`190 192`	`3`
`STRAND`	`194 196`	`3`
`STRAND`	`208 213`	`6`
`TURN`	`214 216`	`3`
`STRAND`	`217 231`	`15`
`HELIX`	`233 235`	`3`
`STRAND`	`237 245`	`9`
`STRAND`	`256 259`	`4`
`STRAND`	`262 273`	`12`
`TURN`	`274 276`	`3`
`STRAND`	`277 284`	`8`
`HELIX`	`285 292`	`8`
`STRAND`	`294 296`	`3`

Sequence information

Length: 297 AA [This is the length of the unprocessed precursor]

Molecular weight: 29663 Da [This is the MW of the unprocessed precursor]

CRC64: 7F6CF04A81B4B3C9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTFKRFSPLS STSRYARLLA VASGLVAAAA LATPSAVAAP EAESKATVSQ LADASSAILA 

        70         80         90        100        110        120 
ADVAGTAWYT EASTGKIVLT ADSTVSKAEL AKVSNALAGS KAKLTVKRAE GKFTPLIAGG 

       130        140        150        160        170        180 
EAITTGGSRC SLGFNVSVNG VAHALTAGHC TNISASWSIG TRTGTSFPNN DYGIIRHSNP 

       190        200        210        220        230        240 
AAADGRVYLY NGSYQDITTA GNAFVGQAVQ RSGSTTGLRS GSVTGLNATV NYGSSGIVYG 

       250        260        270        280        290 
MIQTNVCAEP GDSGGSLFAG STALGLTSGG SGNCRTGGTT FYQPVTEALS AYGATVL

P00776 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools