Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Extracellular small neutral protease

Gene

snpA

Organism
Streptomyces caespitosus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Specifically hydrolyzes the peptide bond at the imino side of aromatic residues.

Catalytic activityi

Hydrolyzes proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca2+ ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761Calcium
Metal bindingi78 – 781Calcium
Metal bindingi83 – 831Zinc; catalytic
Active sitei84 – 841
Metal bindingi87 – 871Zinc; catalytic
Metal bindingi93 – 931Zinc; catalytic

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM07.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular small neutral protease (EC:3.4.24.77)
Alternative name(s):
SCNP
Snapalysin
Gene namesi
Name:snpA
OrganismiStreptomyces caespitosus
Taxonomic identifieri53502 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 132132Extracellular small neutral proteasePRO_0000078176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 1121 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi12 – 143Combined sources
Helixi15 – 2814Combined sources
Beta strandi30 – 367Combined sources
Beta strandi41 – 477Combined sources
Beta strandi54 – 574Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 686Combined sources
Helixi69 – 746Combined sources
Helixi77 – 8913Combined sources
Helixi102 – 1043Combined sources
Turni105 – 1084Combined sources
Helixi119 – 12810Combined sources
Turni129 – 1313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7KX-ray1.00A1-132[»]
1KUHX-ray1.60A1-132[»]
4HX3X-ray2.70A/C/E/G/I/K2-132[»]
SMRiP56406. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56406.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M7 family.Curated

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR000013. Peptidase_M7.
[Graphical view]
PfamiPF02031. Peptidase_M7. 1 hit.
[Graphical view]
PIRSFiPIRSF016573. Peptidase_M7. 1 hit.
PRINTSiPR00787. NEUTRALPTASE.
ProDomiPD016028. Peptidase_M7. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P56406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TVTVTYDPSN APSFQQEIAN AAQIWNSSVR NVQLRAGGNA DFSYYEGNDS
60 70 80 90 100
RGSYAQTDGH GRGYIFLDYQ QNQQYDSTRV TAHETGHVLG LPDHYQGPCS
110 120 130
ELMSGGGPGP SCTNPYPNAQ ERSRVNALWA NG
Length:132
Mass (Da):14,376
Last modified:July 15, 1998 - v1
Checksum:i7CB988AFC2F0B1E4
GO

Sequence databases

PIRiS63978.

Cross-referencesi

Sequence databases

PIRiS63978.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7KX-ray1.00A1-132[»]
1KUHX-ray1.60A1-132[»]
4HX3X-ray2.70A/C/E/G/I/K2-132[»]
SMRiP56406. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM07.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56406.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR000013. Peptidase_M7.
[Graphical view]
PfamiPF02031. Peptidase_M7. 1 hit.
[Graphical view]
PIRSFiPIRSF016573. Peptidase_M7. 1 hit.
PRINTSiPR00787. NEUTRALPTASE.
ProDomiPD016028. Peptidase_M7. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  1. "Complete amino acid sequence of a zinc metalloendoprotease from Streptomyces caespitosus."
    Harada S., Kinoshita T., Kasai N., Tsunasawa S., Sakiyama F.
    Eur. J. Biochem. 233:683-686(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Structure of the zinc endoprotease from Streptomyces caespitosus."
    Kurisu G., Kinoshita T., Sugimoto A., Nagara A., Kai Y., Kasai N., Harada S.
    J. Biochem. 121:304-308(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiSNPA_STRCS
AccessioniPrimary (citable) accession number: P56406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 1, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.