Q8Y5L9 (MURE_LISMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
EC=6.3.2.13

Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	lmo2038

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP-Rule MF_00208
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP-Rule MF_00208
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule 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. HAMAP-Rule MF_00208
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 Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division 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 tetrahydrofolylpolyglutamate biosynthetic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: HAMAP tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 491	491	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208		PRO_0000101911
Regions
	Nucleotide binding	108 – 114	7	ATP Potential
	Region	150 – 151	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	407 – 410	4	Meso-diaminopimelate binding By similarity
	Motif	407 – 410	4	Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208
Sites
	Binding site	30	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	149	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	177	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	183	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	185	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	383	1	Meso-diaminopimelate By similarity
	Binding site	458	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	462	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	217	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y5L9 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 9B80F0F669CFEB95	FASTA	491	53,747
	10 20 30 40 50 60 MKLNELMQAI PVFTGEVSET IEISHIAQDS RKVKPGTLFI CIDGEVVDGH KFASRAVELG 70 80 90 100 110 120 AVAIIAEKQV DVSIPVIYVR DSKRAMAMLA DYFYGSPTQA LKLVGITGTN GKTTVSHLVE 130 140 150 160 170 180 QIVRENGEQT GLIGTMYRKI GDQILETKNT TPDSLTLQET FRDMLLSGVS TAVMEVSSHA 190 200 210 220 230 240 LVQGRVYGSD YDVAVFMNLS QDHLDYHHTM EEYANAKSLL FAQLGNSYHT SNPKIAVLNA 250 260 270 280 290 300 DDAESVRMQK ATAAHIITFG IKQEADFQAS NIKITSHGST FDLGTPVGNF TLKIKMIGNF 310 320 330 340 350 360 SVYNVLAAIA TSFALHIPME KAIKTVESIP GVKGRFELVH AGQEFPVIVD YAHTPDGLLN 370 380 390 400 410 420 VLETIDEFAE KRVFVVVGCG GDRDKGKRPQ MAKIAVDYAT NPIFTSDNPR SENPRAIIED 430 440 450 460 470 480 MIQGVPESDA YVVHENRRDA IRFAVNQAEA GDVILIAGKG HEDYQVVGDE VIDFDDRVEA 490 RIAIEKKLGL A

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591982 Genomic DNA. Translation: CAD00116.1.
PIR	AF1329.
RefSeq	NP_465562.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y5L9.
ModBase	Search...
Protein-protein interaction databases
STRING	169963.lmo2038.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD00116; CAD00116; CAD00116.
GeneID	987940.
KEGG	lmo:lmo2038.
PATRIC	20313275. VBILisMon69206_2086.
Organism-specific databases
GenoList	LMO2038.
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HOG000268118.
KO	K01928.
OMA	HTMEEYA.
ProtClustDB	PRK00139.
Enzyme and pathway databases
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.40.1190.10. 1 hit. 3.90.190.20. 1 hit.
HAMAP	MF_00208. MurE.
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Pfam	PF01225. Mur_ligase. 1 hit. 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_LISMO

Accession

Primary (citable) accession number: Q8Y5L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program