Q9AKP0 (MURE_RICMO) Reviewed, UniProtKB/Swiss-Prot

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):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

Name:

murE

Organism

Rickettsia montana

Taxonomic identifier

33991 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00208
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-Rule MF_00208
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule 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. HAMAP-Rule MF_00208
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
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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: UniProtKB-KW 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 – 479	479	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208		PRO_0000101933
Regions
	Nucleotide binding	98 – 104	7	ATP Potential
	Region	144 – 145	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	396 – 399	4	Meso-diaminopimelate binding By similarity
	Motif	396 – 399	4	Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208
Sites
	Binding site	21	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	171	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	177	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	179	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	372	1	Meso-diaminopimelate By similarity
	Binding site	446	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	450	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	211	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9AKP0 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: F9742817074EB27F	FASTA	479	53,568
	10 20 30 40 50 60 MSHNLKQLFQ QHKVKGLSIN SKTVKDKDVF FAIKGRNTDG NAFIKDALSK GAVLVITDNK 70 80 90 100 110 120 KNIVIDKVIY VKDVQAALHE AIEIFYPKKP KNLIAVTGTN GKSSVVSYIA QTHSLLGKKA 130 140 150 160 170 180 ASIGTIGVEI FGCDNLINDV PELTTLDYLS FRKIAHNLAE NGIEYLVFEA SSHGLDQARL 190 200 210 220 230 240 REIKVNIACF TSFSQDHLDY HHTKENYLLA KLKLFINHLL PNGIAILNSD IEEIEFVKDY 250 260 270 280 290 300 LHNHNIKFIT VGKKGDLEIT RINCSLKGQN INFTFNNREY NFNTPIIGSF QASNLLIAVL 310 320 330 340 350 360 SMHYTGFAFD DVIDSLVEVK AVKGRMERID NTNIFVDYAH TPDALEKALT ELKNIKLHDS 370 380 390 400 410 420 KLSVVFGCGG NRDKAKRSLM GQMAAKRADT IIITDDNPRN EDPKLIRAEI ISGIEKADYT 430 440 450 460 470 EIANREEAIK YGINNLKQDD ILLVAGKGHE NYQIIGDKKL PFDDAEVVRK CVKVCHPVA

References

[1]	"Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes." Andersson J.O., Andersson S.G.E. Mol. Biol. Evol. 18:829-839(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ293315 Genomic DNA. Translation: CAC33608.1.
3D structure databases
ProteinModelPortal	Q9AKP0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.40.1190.10. 1 hit. 3.90.190.20. 1 hit.
HAMAP	MF_00208. MurE.
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_RICMO

Accession

Primary (citable) accession number: Q9AKP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program