Q03415 (ENP1_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	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
Organism	Lysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifier	1421 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Lysinibacillus

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Sporulation
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 396	396	Gamma-D-glutamyl-L-diamino acid endopeptidase 1		PRO_0000212788
Regions
	Repeat	3 – 46	44	LysM 1
	Repeat	53 – 96	44	LysM 2
	Region	101 – 396	296	Catalytic
Sites
	Active site	347	1	Proton donor By similarity
	Active site	366	1	Nucleophile By similarity
	Metal binding	162	1	Zinc By similarity
	Metal binding	165	1	Zinc By similarity
	Metal binding	307	1	Zinc By similarity
	Binding site	255	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03415 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: D929CEBC92324473	FASTA	396	44,724
	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

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.
PIR	S33310.
3D structure databases
ProteinModelPortal	Q03415.
ModBase	Search...
Protein family/group databases
MEROPS	M14.008.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000834. Peptidase_M14. IPR018392. Peptidoglycan-bd_lysin. IPR002482. Peptidoglycan-bd_Lysin_subgr. [Graphical view]
Pfam	PF01476. LysM. 2 hits. PF00246. Peptidase_M14. 1 hit. [Graphical view]
SMART	SM00257. LysM. 2 hits. SM00631. Zn_pept. 1 hit. [Graphical view]
PROSITE	PS00132. CARBOXYPEPT_ZN_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENP1_LYSSH

Accession

Primary (citable) accession number: Q03415

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program