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Q9K0Y9 (MURE_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
Ordered Locus Names:NMB0414
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceInferred 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 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 MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208

Subcellular location

Cytoplasm By similarity HAMAP MF_00208.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101916

Regions

Nucleotide binding114 – 1207ATP Potential
Region156 – 1572UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region413 – 4164Meso-diaminopimelate binding By similarity
Motif413 – 4164Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1891UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3891Meso-diaminopimelate By similarity
Binding site4621Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4661Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2231N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K0Y9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B772F358CA32919E

FASTA49253,045
        10         20         30         40         50         60 
MFSKLTPLAE TGIPTLSCAN AAGRLLHSDS RQIKQGDIFV ACPGEYADGR SYIPAAVANG 

        70         80         90        100        110        120 
AAFVFWDDDG KFAWNPEWKV PNQGIKDLKH RAGILAAQVY GNVSDGLKVW GVAGTNGKTS 

       130        140        150        160        170        180 
ITQWLAQAAD LLGEKTAIVG TVGNGFWGAL EETTHTTPAP VDVQTLLYRF RQQGATVAAM 

       190        200        210        220        230        240 
EVSSHGLDQS RVNGVSFRSA IFTNLTRDHL DYHGTMEAYG AIKSRLFYWH GLKHAVINVD 

       250        260        270        280        290        300 
DEYGAELVGR LKKDCPDLAV YSYGFSEHAD IRITDFTASS DGIAAVFQTP WGEGKCRTRL 

       310        320        330        340        350        360 
LGRFNAQNLA ACIALLCANG YPLDKVLDVL AKIRPASGRM DCIMNSGKPL VVVDYAHTPD 

       370        380        390        400        410        420 
ALEKALATLQ EIKPQGAALW CVFGCGGNRD RGKRPLMGAA AVQGADKVVV TSDNPRLENP 

       430        440        450        460        470        480 
HDIINDILPA VPAPECVEAD RAAAVRYAVE QAAANDIILI AGKGHENYQD VQGVKHRFSD 

       490 
LEIVGQALLT RK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002098 Genomic DNA. Translation: AAF40853.1.
PIRC81202.
RefSeqNP_273463.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9K0Y9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000009862; EBNEIP00000009482; EBNEIG00000009862.
GeneID902530.
GenomeReviewsGene locus NMB0414 in contig AE002098_GR.
KEGGnme:NMB0414.
NMPDRfig|122586.1.peg.397.
PATRIC20356017. VBINeiMen85645_0524.
TIGRNMB0414.

Phylogenomic databases

GeneTreeEBGT00050000020540.
HOGENOMHBG602753.
OMASCANAAG.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0414-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KOK01928.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. MurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_NEIMB
AccessionPrimary (citable) accession number: Q9K0Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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