Reviewed, UniProtKB/Swiss-Prot Q04Y85 (MURE_LEPBL)

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

Gene names

Name:	murE
Ordered Locus Names:	LBL_2600

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]

Taxonomic identifier

355276 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	500 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 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 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.

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-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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 – 500	500	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_1000012371
Regions
	Nucleotide binding	118 – 124	7	ATP Potential
	Region	160 – 161	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	419 – 422	4	Meso-diaminopimelate binding By similarity
	Motif	419 – 422	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	38	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
	Binding site	395	1	Meso-diaminopimelate By similarity
	Binding site	471	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	475	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	227	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04Y85-1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 7956C64A14928D2C	FASTA	500	54,801
	10 20 30 40 50 60 MKMKLTNLLH EFPELKLGSL PSGKNPDSVP IEYIQSDSRK TNPEDIFCVP ESIGTKKGEF 70 80 90 100 110 120 ISNTKASVIL LHRSSNISID SSKIVLECEE DPEQLQGRIA SFLLGHPSKT LEIVAVTGTN 130 140 150 160 170 180 GKTSLTNILF ALAKDQGKIC GLIGTIGVKF GDRSIDTGYT TPDASSLNLI LKQMKDEGVT 190 200 210 220 230 240 TVFMEASSHG LKLGRIGGIS LKAGVFTNLT QDHLDFHSDM EDYFESKFRL FEILDVSKSP 250 260 270 280 290 300 FAVLDYSSPG GNELHRKIRN NLPDLPIKAL DGIGGEYKVS NPFLTLQGTS YVLSLPGNRS 310 320 330 340 350 360 QTISTNLLGS FNVRNTALAF LTGLGLGLDP KGMFSSLKEI PQIPGRFQIV YSKDRSRMAV 370 380 390 400 410 420 VDYAHTPDAL ENIIRSVRNS RPKRLITLFG CGGDRDKTKR PKMARIAEEL SDQVILTSDN 430 440 450 460 470 480 PRSEKPEAIL DEIQSGFSPG FTPLLREVDR ARAISEGVGI LPEGGCLLVA GKGHEEYQII 490 500 GKEKRHFSDV EEVRKAFGLF

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000348 Genomic DNA. Translation: ABJ79960.1.
RefSeq	YP_798893.1.
3D structure databases
SMR	Q04Y85. Positions 27-499.
ModBase	Search...
Protein-protein interaction databases
STRING	Q04Y85.
Genome annotation databases
GeneID	4407945.
GenomeReviews	Gene locus LBL_2600 in contig CP000348_GR.
KEGG	lbl:LBL_2600.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HBG602753.
OMA	HTPDGIE.
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_LEPBL

Accession

Primary (citable) accession number: Q04Y85

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	February 9, 2010
This is version 29 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)