Reviewed, UniProtKB/Swiss-Prot Q72R81 (MURE_LEPIC)

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:	LIC_11867

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni [Complete proteome] [HAMAP]

Taxonomic identifier

44275 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	506 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 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.
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.
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-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 – 506	506	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_0000101907
Regions
	Nucleotide binding	124 – 130	7	ATP Potential
	Region	166 – 167	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	425 – 428	4	Meso-diaminopimelate binding By similarity
	Motif	425 – 428	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	38	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	193	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	201	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	401	1	Meso-diaminopimelate By similarity
	Binding site	477	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	481	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	233	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72R81-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 387BF2B1E2142043	FASTA	506	56,318
	10 20 30 40 50 60 MKMKLTSLLL KFPEIKLKSF PSGKNPDSIE IEYIQSDSRK TNKNDIFCVA DSIGSKKKEF 70 80 90 100 110 120 ISNAKASLIL LRTDSNVLND LLEVMNSSKI FLECEIDPEQ LQGRIASFLL GHPSKDLDIV 130 140 150 160 170 180 AVTGTNGKTS LTNILFSLAK DQGINCGLIG TIGVKFGDRV IDTGYTTPDA SSLNLILKEM 190 200 210 220 230 240 KEEGITTVFM EASSHGLKLG RMNGISVRAG VFTNLTQDHL DFHSDMEDYF ESKFRLFEIL 250 260 270 280 290 300 DFSKSTFAVL DYSAPNGSKL YHKILNRFPD LLIYALDDIY RKWKISDISL NLQGTSYVLG 310 320 330 340 350 360 LPGNQERKIS TNLLGSFNVR NTALAFLTGI GIGLDLEKMS NSLEKIPQIP GRFQIIYSKD 370 380 390 400 410 420 RSRMAVVDYA HTPDALENII RSVRDSQPKC LITLFGCGGD RDRTKRPKMA RIAEELSDQV 430 440 450 460 470 480 ILTSDNPRTE KPETILDEIQ TGFSSGFIPL LREVDRAKAI VEGISCLPEG GCLLVAGKGH 490 500 EEYQIIGKEK RHFSDVEEVQ KAFGLF

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed: 15028702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016823 Genomic DNA. Translation: AAS70453.1.
RefSeq	YP_001816.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2770780.
GenomeReviews	Gene locus LIC_11867 in contig AE016823_GR.
KEGG	lic:LIC11867.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q72R81.
OMA	HTPDGIE.
Enzyme and pathway databases
BioCyc	LINT267671:LIC_11867-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_LEPIC

Accession

Primary (citable) accession number: Q72R81

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 46 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)