Reviewed, UniProtKB/Swiss-Prot P59419 (MURE_BUCBP)

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:	bbp_203

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	508 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 – 508	508	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_0000101875
Regions
	Nucleotide binding	121 – 127	7	ATP Potential
	Region	163 – 164	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	423 – 426	4	Meso-diaminopimelate binding By similarity
	Motif	423 – 426	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	33	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	162	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	190	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	196	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	198	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	399	1	Meso-diaminopimelate By similarity
	Binding site	474	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	478	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	230	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59419-1 [UniParc]. Last modified March 28, 2003. Version 1. Checksum: B69747808687D18F	FASTA	508	58,577
	10 20 30 40 50 60 MTILIKNNNL QQLLSSWIKL SYSYTISGIQ SDSRLVKPGY LFCVLKKKNI NETNKHMIHA 70 80 90 100 110 120 IKNGAKIILY DTKQKFKNGT LKKIINHVPI IYFFKLSKNL PQILKKYYHF ENNFTLIGIT 130 140 150 160 170 180 GTNGKSTTTH IVSQWANLLN VKIGIMGTLG HGINNNLKKT DNTTESSANI HQFLYHMLKQ 190 200 210 220 230 240 NIKTFAIEIS SHGIVQHRIE QLPFKIAILT NITPEHLDYH RTMDNYINAK KAFFFKYNIN 250 260 270 280 290 300 TLIINADDLI AKTWIKKLNH KNVITITTKD QNFNSISPKK WIHANKIIQK QNCTNIHFNS 310 320 330 340 350 360 SWGHGILNST LIGHFNVINI LLALATLLEL NYPITDLVKV CKYIKTISGR MEHIHIVNKP 370 380 390 400 410 420 KVIIDYAHNT NGLKNLLSTL KEIFNKKKIW CIFGCGGDRD KTKRPYMGSI AEKMSDQVIL 430 440 450 460 470 480 TNDNPRNEHP LKIIKNILSG CKFKNKIRII PNREHAIKFA VNNADKEDII VVAGKGHEKY 490 500 QIINNKYYHF SDHKIIKKLL NKKNYDFN

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26935.1.
RefSeq	NP_777830.1.
3D structure databases
HSSP	HSSP built from PDB template 1E8C based on UniProtKB P22188.
ModBase	Search...
Genome annotation databases
GeneID	1058584.
GenomeReviews	Gene locus bbp_203 in contig AE016826_GR.
KEGG	bab:bbp203.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P59419.
OMA	HTPDGIE.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_203-MON.
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_BUCBP

Accession

Primary (citable) accession number: P59419

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	November 3, 2009
This is version 54 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)