Reviewed, UniProtKB/Swiss-Prot Q8CWQ5 (MURE_STRR6)

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:	spr1384

Organism

Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Complete proteome] [HAMAP]

Taxonomic identifier

171101 [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_0000101954
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)
	Q8CWQ5-1 [UniParc]. Last modified March 1, 2003. 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 of the bacterium Streptococcus pneumoniae strain R6." Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. , Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., Glass J.I. J. Bacteriol. 183:5709-5717(2001) [PubMed: 11544234] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE007317 Genomic DNA. Translation: AAL00188.1.
PIR	G98044.
RefSeq	NP_358977.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	934603.
GenomeReviews	Gene locus spr1384 in contig AE007317_GR.
KEGG	spr:spr1384.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8CWQ5.
OMA	Q8CWQ5. HTPDGIE.
Enzyme and pathway databases
BioCyc	SPNE171101:SPR1384-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_STRR6

Accession

Primary (citable) accession number: Q8CWQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 44 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)