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Q03415 (ENP1_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-D-glutamyl-L-diamino acid endopeptidase 1

EC=3.4.19.11
Alternative name(s):
Endopeptidase I
Gamma-D-glutamyl-L-diamino acid endopeptidase I
Gamma-D-glutamyl-meso-diaminopimelate peptidase I
OrganismLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifier1421 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

An endopeptidase which hydrolyzes the gamma-D-Glu-(L)meso-diaminopimelic acid bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. It is active on spore cortex peptidoglycan.

Catalytic activity

Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted.

Cofactor

Zinc.

Developmental stage

Produced at stage IV of sporulation in forespore and spore integuments.

Domain

LysM repeats are thought to be involved in peptidoglycan binding.

Sequence similarities

Belongs to the peptidase M14 family.

Contains 2 LysM repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Gamma-D-glutamyl-L-diamino acid endopeptidase 1
PRO_0000212788

Regions

Repeat3 – 4644LysM 1
Repeat53 – 9644LysM 2
Region101 – 396296Catalytic

Sites

Active site3471Proton donor By similarity
Active site3661Nucleophile By similarity
Metal binding1621Zinc By similarity
Metal binding1651Zinc By similarity
Metal binding3071Zinc By similarity
Binding site2551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03415 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: D929CEBC92324473

FASTA39644,724
        10         20         30         40         50         60 
MDILIRPGDS LWYFSDLFKI PLQLLLDSNR NINPQLLQVG QRIQIPGYVT TSYTITQGDS 

        70         80         90        100        110        120 
LWQIAQNKNL PLNAILLVNP EIQPSRLHIG QTIQVPQRLT WRLVNGQQNY DYSMMMNDIK 

       130        140        150        160        170        180 
KLQTAYPFLQ GTPIGNSVLA QPIPEILIGN GSKRIHYKAS FHANEWITTP IIMTFLNDYL 

       190        200        210        220        230        240 
LALTNQTTIR GLSMGPLYNQ TTLSLVPMVN PDGVNLVING PPANEALKNK LIAWNHNSQN 

       250        260        270        280        290        300 
FSGWKANING VDLNDQFPAK WELENARNPQ TPGPRDYGGE APLTQPEAIA MADLTRSRNF 

       310        320        330        340        350        360 
AWVLAFHTQG RVIYWGFENL EPPESQTMVE EFSRVSGYEP IQSANSYAGY KDWFIQDWRR 

       370        380        390 
PGFTVELGSG TNPLPISEFD TIYQEALGIF LAGLYL 

« Hide

References

[1]"Characterization of the sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein."
Hourdou M.-L., Guinand M., Vacheron M.J., Michel G., Denoroy L., Duez C.M., Englebert S., Joris B., Weber G., Ghuysen J.-M.
Biochem. J. 292:563-570(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: DSM 396 / NCTC 9602.
[2]"Purification and partial characterization of the extracellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602."
Garnier M., Vacheron M., Guinard J.-M., Michel G.
Eur. J. Biochem. 148:539-543(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: DSM 396 / NCTC 9602.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69507 Genomic DNA. Translation: CAA49259.1.
PIRS33310.

3D structure databases

ProteinModelPortalQ03415.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM14.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.350.10. 2 hits.
InterProIPR018392. LysM_dom.
IPR000834. Peptidase_M14.
[Graphical view]
PfamPF01476. LysM. 2 hits.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
SMARTSM00257. LysM. 2 hits.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMSSF54106. SSF54106. 2 hits.
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENP1_LYSSH
AccessionPrimary (citable) accession number: Q03415
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries