Reviewed, UniProtKB/Swiss-Prot P45060 (MURE_HAEIN)

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:	HI1133

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	488 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 – 488	488	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_0000101900
Regions
	Nucleotide binding	113 – 119	7	ATP Potential
	Region	41 – 43	3	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	155 – 156	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	410 – 413	4	Meso-diaminopimelate binding By similarity
	Motif	410 – 413	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	24	1	UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
	Binding site	26	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	154	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	182	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	188	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	190	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	386	1	Meso-diaminopimelate By similarity
	Binding site	461	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	465	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	222	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45060-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 46E20FF7491BC45A	FASTA	488	53,523
	10 20 30 40 50 60 MKKLTALFNL PELKNDIELH NMVLDSRKVK AGDLFVAIKG HQVDGNQFID SALHSGASAV 70 80 90 100 110 120 VSETELSSEH LTVAFIGNVP VVKYYQLAHH LSSLADVFYD SPSNNLTLVG VTGTNGKTTI 130 140 150 160 170 180 SQLLAQWAEL LGHRAAVMGT IGNGLFGQIV EAKNTTGSAV EIQSSLSAFK HAGADFTSIE 190 200 210 220 230 240 VSSHGLAQHR VEALHFKAAI FTNLTRDHLD YHQSMENYAA AKKRLFTELD TQIKVINADD 250 260 270 280 290 300 EIGYQWLTEL PDAIAVSMNA DFKVGSHQWM KAINIHYHFK GADITFESSW GNGVLHSPLI 310 320 330 340 350 360 GAFNVSNLLL VMTTLLSFGY PLENLLATAK SLKGVCGRME MIQYPNKPTV IVDYAHTPDA 370 380 390 400 410 420 LEKALIAARE HCQGELWCIF GCGGDRDRGK RPLMAQVAEQ FAEKIIVTKD NPRTESQSQI 430 440 450 460 470 480 ETDIVAGFKN MEKVGIIPDR AQAIQFAIES AVENDVILIA GKGHEHYQII GSEVVHFSDQ EIALDFLK

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22788.1.
PIR	H64184.
RefSeq	NP_439291.1.
3D structure databases
HSSP	HSSP built from PDB template 1E8C based on UniProtKB P22188.
ModBase	Search...
Genome annotation databases
GeneID	949983.
GenomeReviews	Gene locus HI1133 in contig L42023_GR.
KEGG	hin:HI1133.
NMPDR	fig|71421.1.peg.1086.
TIGR	HI1133.
Phylogenomic databases
HOGENOM	P45060.
OMA	HTPDGIE.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1133-MON.
BRENDA	6.3.2.13. 109.
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_HAEIN

Accession

Primary (citable) accession number: P45060

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 73 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)