Reviewed, UniProtKB/Swiss-Prot A7FTY1 (MURE_CLOB1)

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:	CLB_1482

Organism

Clostridium botulinum (strain ATCC 19397 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

441770 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	483 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 – 483	483	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_1000012347
Regions
	Nucleotide binding	112 – 118	7	ATP Potential
	Region	154 – 155	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	404 – 407	4	Meso-diaminopimelate binding By similarity
	Motif	404 – 407	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	29	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	181	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	189	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	380	1	Meso-diaminopimelate By similarity
	Binding site	454	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	458	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	221	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7FTY1-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 6D6B564E45A4A88C	FASTA	483	54,678
	10 20 30 40 50 60 MNLNLILKSL EYSFIKENKK EIEKIEYDSR KVKEGDLFVC IEGYATDGHK YAKKAYDNGA 70 80 90 100 110 120 KVIVCEKDLE DLSYYKDCTI IKVSDSRKAL AIMSSNYYGN PSKHIKIIGI TGTNGKTTST 130 140 150 160 170 180 FMMKAILEKA GYKVGLLGTI ANYIGNKKIE SHRTTPESLE LQKLFKDMVD EKVDYCVMEV 190 200 210 220 230 240 SSHSLYLDRV YGVEFKEAIF TNLTQDHLDF HKTFENYFNS KLILFKNAQN SVINIDDSYG 250 260 270 280 290 300 EKVLKKALGN KITYGVEKNC DLKAENLHMH SRGVEFDTIF KNEKETIALN IPGKYNIYNA 310 320 330 340 350 360 LGSIGACLLE GIPLKTIKEA LEDMPSVPGR CEIVTKNYNL GYDVIVDYAH TPDGLENILN 370 380 390 400 410 420 TAREFTKGRL ISVYGCGGDR DRTKRPIMGK VGSNLSDIAI ITSDNPRTED PKLIIKDVLE 430 440 450 460 470 480 GIERDNYIVV EGRRDAIRKA MEIAKENDVI VVAGKGHEDY QILKDKTIHF DEREVIEELI KEI

References

[1]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000726 Genomic DNA. Translation: ABS32867.1.
RefSeq	YP_001383808.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7FTY1.
Genome annotation databases
GeneID	5396221.
GenomeReviews	Gene locus CLB_1482 in contig CP000726_GR.
KEGG	cba:CLB_1482.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	NPRSENE.
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_CLOB1

Accession

Primary (citable) accession number: A7FTY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 11, 2007
Last modified:	November 3, 2009
This is version 19 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)