Reviewed, UniProtKB/Swiss-Prot Q1JID8 (MURE_STRPD)

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

Gene names

Name:	murE
Ordered Locus Names:	MGAS10270_Spy0320

Organism

Streptococcus pyogenes serotype M2 (strain MGAS10270) [Complete proteome] [HAMAP]

Taxonomic identifier

370552 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Post-translational modification	Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity.
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 cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP 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_1000012388
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	158	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)
	Q1JID8-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: B630BA6E4E7F51E3	FASTA	481	53,479
	10 20 30 40 50 60 MITIEQLLDI LKKDHNFREV LDADGYHYHY QGLSFERLSY DSRQVDGKTL FFAKGATFKA 70 80 90 100 110 120 DYLKEAITNG LQLYISEVDY ELGIPVVLVT DIKKAMSLIA MAFYGNPQEK LKLLAFTGTK 130 140 150 160 170 180 GKTTAAYFAY HMLKESYKPA MFSTMNTTLD GKTFFKSQLT TPESLDLFAM MAECVTNGMT 190 200 210 220 230 240 HLIMEVSSQA YLVDRVYGLT FDVGVFLNIS PDHIGPIEHP TFEDYFYHKR LLMENSRAVV 250 260 270 280 290 300 INSGMDHFSF LADQVADQEH VFYGPLSDNQ ITTSQAFSFE AKGQLAGHYD IQLIGHFNQE 310 320 330 340 350 360 NAMAAGLACL RLGASLADIQ KGIAKTRVPG RMEVLTMTNH AKVFVDYAHN GDSLEKLLSV 370 380 390 400 410 420 VEEHQTGKLM LILGAPGNKG ESRRADFGRV IHQHPNLTVI LTADDPNFED PEDISKEIAS 430 440 450 460 470 480 HIARPVEIIS DREQAIQKAM SLCQGAKDAV IIAGKGADAY QIVKGQQVAY AGDLAIAKHY L

References

[1]

"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus." Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M. Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed: 16636287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000260 Genomic DNA. Translation: ABF33385.1.
RefSeq	YP_597929.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4064307.
GenomeReviews	Gene locus murE in contig CP000260_GR.
KEGG	sph:MGAS10270_Spy0320.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1JID8.
OMA	Q1JID8. HTPDGIE.
Enzyme and pathway databases
BioCyc	SPYO370552:MGAS10270_SPY0320-MON.
Family and domain databases
HAMAP	MF_00208. [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.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_STRPD

Accession

Primary (citable) accession number: Q1JID8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 13, 2006
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)