Reviewed, UniProtKB/Swiss-Prot Q9A196 (MURE_STRP1)

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:	SPy_0388, M5005_Spy0325

Organism

Streptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]

Taxonomic identifier

301447 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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. Ref.3
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.
Biophysicochemical properties	Kinetic parameters: KM=20.5 µM for UDP-N-acetylmuramoyl-L-Ala-D-Glu HAMAP MF_00208 KM=122 µM for L-lysine KM=125 µM for ATP Temperature dependence: Optimum temperature is 28 degrees Celsius.

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: 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_0000101955
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)
	Q9A196-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 80DB99E64BB23708	FASTA	481	53,513
	10 20 30 40 50 60 MITIEQLLDI LKKDHNFREV LDADGYHYHY QGFSFERLSY 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of an M1 strain of Streptococcus pyogenes." Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E. Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed: 11296296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700294 / SF370 / Serotype M1.
[2]	"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events." Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M. J. Infect. Dis. 192:771-782(2005) [PubMed: 16088826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.
[3]	"Cloning, expression and characterization of the Streptococcus pyogenes murE gene encoding a UDP-MurNAc-L-alanyl-D-glutamate: L-lysine ligase." Triolo T.A., Chabin R.M., Pompliano D.L. Enzyme Microb. Technol. 35:300-308(2004) Cited for: FUNCTION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 700294 / SF370 / Serotype M1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004092 Genomic DNA. Translation: AAK33428.1. CP000017 Genomic DNA. Translation: AAZ50944.1.
RefSeq	NP_268707.1. YP_281689.1.
3D structure databases
SMR	Q9A196. Positions 2-455, 32-480.
ModBase	Search...
Genome annotation databases
GeneID	3572576. 900656.
GenomeReviews	Gene locus SPy_0388 in contig AE004092_GR. Gene locus M5005_Spy0325 in contig CP000017_GR.
KEGG	spy:SPy_0388. spz:M5005_Spy_0325.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG351099.
OMA	HTPDGIE.
Enzyme and pathway databases
BioCyc	SPYO160490:SPY0388-MONOMER. SPYO293653:M5005_SPY0325-MONOMER.
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.
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_STRP1

Accession

Primary (citable) accession number: Q9A196
Secondary accession number(s): Q490M4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 63 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)