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Q65JY4 (MURE_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. 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:BLi01735, BL02239
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length488 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 – 488488UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012339

Regions

Nucleotide binding109 – 1157ATP Potential
Region151 – 1522UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region408 – 4114Meso-diaminopimelate binding By similarity
Motif408 – 4114Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site311UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1501UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1781UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3841Meso-diaminopimelate By similarity
Binding site4581Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4621Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65JY4 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 5503B7E1C159504E

FASTA48853,242
        10         20         30         40         50         60 
MKLTKLLTYL KNVPSYAGQE DPDITSIEMD SREVKTGSLF VCIKGYTVDG HDYARQAAEK 

        70         80         90        100        110        120 
GAAAIVAERE VDADVPVIII RHTKRALAVL SDAFYGQPTK QLRLIGITGT NGKTSTSHMV 

       130        140        150        160        170        180 
EEIFRKAGSR TGLIGTMYTK IHDETFEAKN TTPESVTLQK TFRKMVDQGV DTAVMEVSSH 

       190        200        210        220        230        240 
ALHMGRVHGC DYDIAAFTNL TQDHLDYHET MEEYKHAKSL LFSQLGGSFN HETPKWAVLN 

       250        260        270        280        290        300 
ADDPASAYFA QVTSAHLLTY GIQNDADVMA ENIKMAPKGT TFDLVTPKGS AQVTIPLVGL 

       310        320        330        340        350        360 
FNVYNVLTAA AIAIAADIPF ATITEGIEGL KGVRGRFELV DAGQDFPVIV DYAHTPDSLE 

       370        380        390        400        410        420 
NVLNTCRGLT EGKLFVVVGC GGDRDKTKRP KMAKIAVDLA DEPVFTADNP RSENPLAILN 

       430        440        450        460        470        480 
DMEEGVKGAY YHSIVNREQA IFFAIANAKK GDVVLIAGKG HETYQQIGGQ TFDFDDAEVA 


KRAILELK

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References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000002 Genomic DNA. Translation: AAU23273.1.
AE017333 Genomic DNA. Translation: AAU40630.1.
RefSeqYP_006713115.1. NC_006322.1.
YP_078911.1. NC_006270.3.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
ProteinModelPortalQ65JY4.
ModBaseSearch...

Protein-protein interaction databases

STRING279010.BL02239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU23273; AAU23273; BL02239.
AAU40630; AAU40630; BLi01735.
GeneID3030883.
3099138.
KEGGbld:BLi01735.
bli:BL02239.
PATRIC18949069. VBIBacLic203714_1738.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAMAKDNGA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-1721-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_BACLD
AccessionPrimary (citable) accession number: Q65JY4
Secondary accession number(s): Q62VD5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: May 1, 2013
This is version 78 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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