Q04JL8 (MURE_STRP2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
EC=6.3.2.7

Alternative name(s):
L-lysine-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	SPD_1359

Organism

Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP]

Taxonomic identifier

373153 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP MF_00208
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine. HAMAP MF_00208
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208
Subcellular location	Cytoplasm By similarity HAMAP MF_00208.
Post-translational modification	Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208
Sequence similarities	Belongs to the MurCDEF family. MurE subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase HAMAP MF_00208		PRO_1000012386
Regions
	Nucleotide binding	118 – 124	7	ATP Potential
	Region	160 – 161	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Motif	404 – 407	4	L-lysine recognition motif HAMAP MF_00208
Sites
	Binding site	42	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	187	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	195	1	UDP-MurNAc-L-Ala-D-Glu By similarity
Amino acid modifications
	Modified residue	229	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04JL8 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 9A668127E05341E5	FASTA	481	53,828
	10 20 30 40 50 60 MIKIETVLDI LKKDGLFREI IDQGHYHYNY SKVIFDSISY DSRKVTEDTL FFAKGAAFKK 70 80 90 100 110 120 EYLLSAITQG LAWYVAEKDY EVDIPVIIVN DIKKAMSLIA MEFYGNPQEK LKLLAFTGTK 130 140 150 160 170 180 GKTTATYFAY NILSQGHRPA MLSTMNTTLD GETFFKSALT TPESIDLFDM MNQAVQNDRT 190 200 210 220 230 240 HLIMEVSSQA YLVHRVYGLT FDVGVFLNIT PDHIGPIEHP SFEDYFYHKR LLMENSRAVI 250 260 270 280 290 300 INSDMDHFSV LKEQVEDQDH DFYGSQFDNQ IENSKAFSFS ATGKLAGDYD IQLIGNFNQE 310 320 330 340 350 360 NAVAAGLACL RLGASLEDIK KGIAATRVPG RMEVLTQKNG AKVFIDYAHN GDSLKKLINV 370 380 390 400 410 420 VETHQTGKIA LVLGSTGNKG ESRRKDFGLL LNQHPEIQVF LTADDPNYED PMAIADEISS 430 440 450 460 470 480 YINHPVEKIA DRQEAIKAAM AITNHELDAV IIAGKGADCY QIIQGKKESY PGDTAVAENY L

References

[1]

"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6." Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E. J. Bacteriol. 189:38-51(2007) [PubMed: 17041037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D39 / NCTC 7466.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000410 Genomic DNA. Translation: ABJ54578.1.
RefSeq	YP_816820.1. NC_008533.1.
3D structure databases
ProteinModelPortal	Q04JL8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q04JL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000019625; EBSTRP00000018865; EBSTRG00000019625.
GeneID	4442610.
GenomeReviews	Gene locus SPD_1359 in contig CP000410_GR.
KEGG	spd:SPD_1359.
PATRIC	19683944. VBIStrPne27904_1505.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0769.
GeneTree	EBGT00050000027196.
HOGENOM	HBG351099.
OMA	IGTIANY.
ProtClustDB	PRK14022.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K05362.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMs	TIGR01085. MurE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_STRP2

Accession

Primary (citable) accession number: Q04JL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program