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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)DescriptionActionsGraphical viewLength
Metal bindingi76Calcium1 Publication1
Metal bindingi78Calcium1 Publication1
Metal bindingi83Zinc; catalytic1 Publication1
Active sitei841
Metal bindingi87Zinc; catalytic1 Publication1
Metal bindingi93Zinc; catalytic1 Publication1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000781761 – 132Extracellular small neutral proteaseAdd BLAST132

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi99 ↔ 1122 Publications

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1132
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Helixi12 – 14Combined sources3
Helixi15 – 28Combined sources14
Beta strandi30 – 36Combined sources7
Beta strandi41 – 47Combined sources7
Beta strandi54 – 57Combined sources4
Beta strandi59 – 61Combined sources3
Beta strandi63 – 68Combined sources6
Helixi69 – 74Combined sources6
Helixi77 – 89Combined sources13
Helixi102 – 104Combined sources3
Turni105 – 108Combined sources4
Helixi119 – 128Combined sources10
Turni129 – 131Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7KX-ray1.00A1-132[»]
1KUHX-ray1.60A1-132[»]
4HX3X-ray2.70A/C/E/G/I/K2-132[»]
ProteinModelPortaliP56406.
SMRiP56406.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7KX-ray1.00A1-132[»]
1KUHX-ray1.60A1-132[»]
4HX3X-ray2.70A/C/E/G/I/K2-132[»]
ProteinModelPortaliP56406.
SMRiP56406.
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: November 2, 2016
This is version 92 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.