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O85298 (MURE_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative 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:BUsg_215
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceUncertain

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.

Caution

Could be the product of a pseudogene.

Sequence caution

The sequence AE013218 differs from that shown. Reason: Frameshift at position 379. This is probably a pseudogene resulting from truncation by frameshift mutation, as it is possible that this bacterium does not produce peptidoglycan.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Putative UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101874

Regions

Nucleotide binding116 – 1227ATP Potential
Region158 – 1592UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region416 – 4194Meso-diaminopimelate binding By similarity
Motif416 – 4194Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site271UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1571UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1931UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3921Meso-diaminopimelate By similarity
Binding site4671Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4711Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2251N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O85298 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 8AF84E42B4F77511

FASTA49756,842
        10         20         30         40         50         60 
MKKNNLKYIL FPWIKNTPQK KFSNLSLDSR KLTSKDVFIA IKGTKKDGND FIFEAVKKRV 

        70         80         90        100        110        120 
VAILSETKEK KKHGEINYIN NIPILSFFKL SEKISNLAAR VYKEPAKTLK IIGVTGTNGK 

       130        140        150        160        170        180 
TTVTQLINQW SELLGKKIAT MGTLGNGFYN ALKTTKNTTS SAIDIQSFLH IAAKKKINLV 

       190        200        210        220        230        240 
TMEVSSHGLV QNRVKNIPFY IGIFTNLTQD HLDYHKNMKQ YESAKWSFFS QHKIKKIILN 

       250        260        270        280        290        300 
ANDKYAKKWL RKLSDKYTIA VTIQNEKQKK YSTKWINATG IKYNVNSTDV EFESSWGQGI 

       310        320        330        340        350        360 
LSTCLIGYFN IQNLLLSFAS MLEMNYKLSD LINTSIQLQP ILGRMQKFDV FGKPKVIIDY 

       370        380        390        400        410        420 
AHTPDALKKA LNAIKSYYKK KIWCIFGCGG ERDQTKRPLM GSISEKIADR VIITNDNPRN 

       430        440        450        460        470        480 
ENQNKIIKEI VQGCIKKEKI IIIPNREKAI SSTFFKANID DIIFISGKGH ENQQIIKNKI 

       490 
INYSDQKVVI KLLEKKI

« Hide

References

« Hide 'large scale' references
[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.
[2]"Sequence analysis of a DNA fragment from Buchnera aphidicola (Aphid endosymbiont) containing the genes dapD-htrA-ilvI-ilvH-ftsL-ftsI-murE."
Thao M.L., Baumann P.
Curr. Microbiol. 37:214-216(1998) [PubMed: 9688822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-292.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013218 Genomic DNA. No translation available.
AF060492 Genomic DNA. Translation: AAC32338.1.

3D structure databases

ProteinModelPortalO85298.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus BUsg_215 in contig AE013218_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAGALAYVD.

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.
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_BUCAP
AccessionPrimary (citable) accession number: O85298
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 30, 2002
Last modified: November 16, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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