Reviewed, UniProtKB/Swiss-Prot Q6D0H8 (MURE_ERWCT)

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:	ECA3820

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	495 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 – 495	495	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_1000012351
Regions
	Nucleotide binding	116 – 122	7	ATP Potential
	Region	44 – 46	3	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	158 – 159	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	414 – 417	4	Meso-diaminopimelate binding By similarity
	Motif	414 – 417	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	27	1	UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
	Binding site	29	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	157	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	185	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	191	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	193	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	390	1	Meso-diaminopimelate By similarity
	Binding site	465	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	469	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	225	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6D0H8-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 06C185731AF0A765	FASTA	495	53,091
	10 20 30 40 50 60 MADRNLRDLL APWVQDAPAC ALREMILDSR VAAAGDLFVA IVGHKADGRR YIPQAIAQGV 70 80 90 100 110 120 AAIVAEADGE AADGTVREMH GVPVVYLSSL NQRLSALAGR FYQQPAEKLQ LIGVTGTNGK 130 140 150 160 170 180 TTTTQLLAQW SQALGEMSAV MGTVGNGLLG RAIPTENTTG SAVDVQQVLS QLVEQGATFA 190 200 210 220 230 240 AMEVSSHGLV QNRVAALPFT AAVFTNLSRD HLDYHGDMES YEAAKWLLFA EHRVGQMIIN 250 260 270 280 290 300 ADDEVGLRWL AKLPDAVAVT MENNLVPGCR GRWLKATQID YHDNGATIAF DSSWGQGEIE 310 320 330 340 350 360 SRLMGAFNVS NMLLALATLL SLGYPLDKLV IAGSQLQPVC GRMEVFHAEG KPTVVVDYAH 370 380 390 400 410 420 TPDALEKALE AARLHCQGKL WCVFGCGGDR DKGKRPLMGG IAEQLADRVV VTDDNPRSEE 430 440 450 460 470 480 PQAIVADILS GLLDAGRVQV IHGRAEAVTS AIMQAQENDV VLVAGKGHED YQLVGNQRLD 490 YSDRITVARL LGVIA

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX950851 Genomic DNA. Translation: CAG76719.1.
RefSeq	YP_051909.1.
3D structure databases
SMR	Q6D0H8. Positions 3-495.
ModBase	Search...
Genome annotation databases
GeneID	2881726.
GenomeReviews	Gene locus ECA3820 in contig BX950851_GR.
KEGG	eca:ECA3820.
NMPDR	fig|218491.3.peg.2465.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6D0H8.
OMA	FPVIVDY.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA3820-MON.
BRENDA	6.3.2.13. 281579.
Family and domain databases
HAMAP	MF_00208. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. 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	PF01225. Mur_ligase. 1 hit. 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_ERWCT

Accession

Primary (citable) accession number: Q6D0H8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 40 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)