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Protein

Gamma-D-glutamyl-L-diamino acid endopeptidase 1

Gene
N/A
Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621ZincBy similarity
Metal bindingi165 – 1651ZincBy similarity
Binding sitei255 – 2551SubstrateBy similarity
Metal bindingi307 – 3071ZincBy similarity
Active sitei347 – 3471Proton donorBy similarity
Active sitei366 – 3661NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell wall biogenesis/degradation, Sporulation

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM14.008.

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifieri1421 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Gamma-D-glutamyl-L-diamino acid endopeptidase 1PRO_0000212788Add
BLAST

Expressioni

Developmental stagei

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

Structurei

3D structure databases

ProteinModelPortaliQ03415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati3 – 4644LysM 1Add
BLAST
Repeati53 – 9644LysM 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni101 – 396296CatalyticAdd
BLAST

Domaini

LysM repeats are thought to be involved in peptidoglycan binding.

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated
Contains 2 LysM repeats.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.10.350.10. 2 hits.
InterProiIPR018392. LysM_dom.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF01476. LysM. 2 hits.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
SMARTiSM00257. LysM. 2 hits.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54106. SSF54106. 2 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03415-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDILIRPGDS LWYFSDLFKI PLQLLLDSNR NINPQLLQVG QRIQIPGYVT
60 70 80 90 100
TSYTITQGDS LWQIAQNKNL PLNAILLVNP EIQPSRLHIG QTIQVPQRLT
110 120 130 140 150
WRLVNGQQNY DYSMMMNDIK KLQTAYPFLQ GTPIGNSVLA QPIPEILIGN
160 170 180 190 200
GSKRIHYKAS FHANEWITTP IIMTFLNDYL LALTNQTTIR GLSMGPLYNQ
210 220 230 240 250
TTLSLVPMVN PDGVNLVING PPANEALKNK LIAWNHNSQN FSGWKANING
260 270 280 290 300
VDLNDQFPAK WELENARNPQ TPGPRDYGGE APLTQPEAIA MADLTRSRNF
310 320 330 340 350
AWVLAFHTQG RVIYWGFENL EPPESQTMVE EFSRVSGYEP IQSANSYAGY
360 370 380 390
KDWFIQDWRR PGFTVELGSG TNPLPISEFD TIYQEALGIF LAGLYL
Length:396
Mass (Da):44,724
Last modified:October 1, 1994 - v1
Checksum:iD929CEBC92324473
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69507 Genomic DNA. Translation: CAA49259.1.
PIRiS33310.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69507 Genomic DNA. Translation: CAA49259.1.
PIRiS33310.

3D structure databases

ProteinModelPortaliQ03415.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM14.008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.10.350.10. 2 hits.
InterProiIPR018392. LysM_dom.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF01476. LysM. 2 hits.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
SMARTiSM00257. LysM. 2 hits.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54106. SSF54106. 2 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiENP1_LYSSH
AccessioniPrimary (citable) accession number: Q03415
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 26, 2014
This is version 83 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

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.