UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase

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Q9A196 (MURE_STRP1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	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: K_M=20.5 µM for UDP-N-acetylmuramoyl-L-Ala-D-Glu Ref.3 K_M=122 µM for L-lysine K_M=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: 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_0000101955

Regions

Nucleotide binding

118 – 124

ATP Potential

Region

160 – 161

UDP-MurNAc-L-Ala-D-Glu binding By similarity

Motif

404 – 407

L-lysine recognition motif HAMAP MF_00208

Sites

Binding site

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

158

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

187

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

195

UDP-MurNAc-L-Ala-D-Glu By similarity

Amino acid modifications

Modified residue

229

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9A196 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 80DB99E64BB23708
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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

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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. 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. NC_002737.1. YP_281689.1. NC_007297.1.
3D structure databases
ProteinModelPortal	Q9A196.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000001312; EBSTRP00000001312; EBSTRG00000001312. EBSTRT00000028129; EBSTRP00000027147; EBSTRG00000028129.
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.
PATRIC	19714533. VBIStrPyo79812_0335.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000027196.
HOGENOM	HBG351099.
OMA	GALAYVD.
ProtClustDB	PRK14022.
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.
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_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:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents