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A6L075 (MURE_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. 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:BVU_1401
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides ›

Protein attributes

Sequence length484 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-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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012340

Regions

Nucleotide binding111 – 1177ATP Potential
Region153 – 1542UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region402 – 4054Meso-diaminopimelate binding By similarity
Motif402 – 4054Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1801UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3781Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2201N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6L075 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: CAEC00C575D9AA16

FASTA48453,283
        10         20         30         40         50         60 
MKLEKIIKGI TVNEIIGDAS QEISGINMDS RLIEPGHIFV AVKGTQTDGH TYIQKAIEKG 

        70         80         90        100        110        120 
ARTVVCENLP ETLIENVTYI KVNDTEDVVG KLATTFYGDP TSKLELVGVT GTNGKTTIAT 

       130        140        150        160        170        180 
LLYNMFRKFG YKTGLISTVC NYIDEEAIPT DHTTPDPITL NKLLGRMADE GCKYAFMEVS 

       190        200        210        220        230        240 
SHSVAQKRIG GLKFAGGIFT NLTRDHLDYH KTVENYLKAK KAFFDGLPKT AFALTNLDDK 

       250        260        270        280        290        300 
NGLVMTQNTK AKVHTYSLRS LSDFKGKVLE DGFEGMLLDI NNVEVNVQFI GRFNASNLLA 

       310        320        330        340        350        360 
VYGAACLLGK KTEEVLLALS TLRPVAGRFD SLRSPKGYTA IVDYAHTPDA LENVLNAIHE 

       370        380        390        400        410        420 
VLNGKGHVIT VVGAGGNRDK GKRPLMAQEA VKQSDKVIIT SDNPRFEEPQ EIINDMLAGL 

       430        440        450        460        470        480 
TKEDMRKVIS IADRKEAIRT ACMLAQAKDV ILVAGKGHEN YQEIKGIKHH FDDKEVLRDI 


FANE

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References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8482 / DSM 1447 / NCTC 11154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000139 Genomic DNA. Translation: ABR39089.1.
RefSeqYP_001298711.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L075.
ModBaseSearch...

Protein-protein interaction databases

STRING435590.BVU_1401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR39089; ABR39089; BVU_1401.
GeneID5302367.
KEGGbvu:BVU_1401.
PATRIC21067660. VBIBacVul85104_1462.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycBVUL435590:GH96-1469-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
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_BACV8
AccessionPrimary (citable) accession number: A6L075
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: May 1, 2013
This is version 51 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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