Reviewed, UniProtKB/Swiss-Prot Q4L525 (MURE_STAHJ)

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:	SH1941

Organism

Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]

Taxonomic identifier

279808 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	494 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 – 494	494	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase HAMAP MF_00208		PRO_1000012384
Regions
	Nucleotide binding	110 – 116	7	ATP Potential
	Region	152 – 153	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Motif	406 – 409	4	L-lysine recognition motif HAMAP MF_00208
Sites
	Binding site	30	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	179	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	187	1	UDP-MurNAc-L-Ala-D-Glu By similarity
Amino acid modifications
	Modified residue	219	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4L525-1 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: 6FC7854CCA8EBF09	FASTA	494	54,177
	10 20 30 40 50 60 MNANELFEKI RVKQVIGTLD INVTDITTDS RTASEGSIFV ASKGYTVDSH KFCQNVVDQG 70 80 90 100 110 120 AKVIVVNHQQ DINGDVTQVI VPDTLRVASL LAHTLYDFPS HQLTTIGVTG TNGKTSIATM 130 140 150 160 170 180 IHLIYRGLGK GSAYLGTNGF QINEHKTRGA NTTPETVSLT KKIKQAVDEN AEAMTMEVSS 190 200 210 220 230 240 HGLSLGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYAVLNN 250 260 270 280 290 300 DDDFSKYLAS VTPYEIFTYG IDHDAQFMAK NIQESLQGVH FDFDTPIGTY SVKTPYVGKF 310 320 330 340 350 360 NISNIMAAMI AVWSKGTSME DIVRVVENLE PVEGRLEVLD PSLPIDLIID YAHTADGMNK 370 380 390 400 410 420 LIDAVKPFVK QKLIFLIGMA GERDLTKTPE MGAVACRADY VIFTPDNPAN DDPKMLTAEL 430 440 450 460 470 480 AKGATHNHYV EFDDRAEGIK HAIDIAEPGD TVVLASKGRE PYQIMPGHIK VPHRDDLIGL 490 EAAYKKFGGG PSEH

References

[1]

"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP006716 Genomic DNA. Translation: BAE05250.1.
RefSeq	YP_253856.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3482035.
GenomeReviews	Gene locus SH1941 in contig AP006716_GR.
KEGG	sha:SH1941.
NMPDR	fig|279808.3.peg.2144.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q4L525.
OMA	Q4L525. HTPDGIE.
Enzyme and pathway databases
BioCyc	SHAE279808:SH1941-MON.
Family and domain databases
HAMAP	MF_00208. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. 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	PF01225. Mur_ligase. 1 hit. 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_STAHJ

Accession

Primary (citable) accession number: Q4L525

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 2, 2005
Last modified:	June 16, 2009
This is version 37 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)