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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:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761Calcium1 Publication
Metal bindingi78 – 781Calcium1 Publication
Metal bindingi83 – 831Zinc; catalytic1 Publication
Active sitei84 – 841
Metal bindingi87 – 871Zinc; catalytic1 Publication
Metal bindingi93 – 931Zinc; catalytic1 Publication

GO - Molecular functioni

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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

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 ↔ 1122 Publications

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[»]
ProteinModelPortaliP56406.
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[»]
ProteinModelPortaliP56406.
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...

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: January 20, 2016
This is version 90 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

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 one 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.