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Q5L0Y0 (MURE_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:GK1115
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length489 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 – 489489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012352

Regions

Nucleotide binding108 – 1147ATP Potential
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region407 – 4104Meso-diaminopimelate binding By similarity
Motif407 – 4104Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1491UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3831Meso-diaminopimelate By similarity
Binding site4591Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4631Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L0Y0 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 7128962AC93C9A2D

FASTA48953,320
        10         20         30         40         50         60 
MKLLTLLSHL PGFWVHHGGN PDIVALEMDS RRVASGSLFF CLKGFTVDGH DFAEEAVARG 

        70         80         90        100        110        120 
AAAIVAERPL SVDVPVVLVS DSRRAMAILA DAFYGRPTHR LHLIGVTGTN GKTTTTSIIE 

       130        140        150        160        170        180 
QIARKTGKKT GLIGTVHIKV GDRSYPAANT TPESLILQRT FKQMVDEGVE FVAMEVSSHA 

       190        200        210        220        230        240 
LHQGRVHGCD YDVAVFTNLT QDHLDYHGTM EEYRNAKGLL FAQLGNRYDE RRPKFAVLNH 

       250        260        270        280        290        300 
DDPVSQYYKH MTAAPIVTYG MREKSDVMAE QIRMTAGGMA FRLCTPHGSA AVETKLVGSF 

       310        320        330        340        350        360 
NVYNILAAAA ACLASGFSLE TIAAALADVE PVPGRFETVD EGQNFTIIVD YAHTPDSLEN 

       370        380        390        400        410        420 
ALKTVRQLAK RNVYVVIGCG GDRDPSKRPL MAQVAVRYAD VAIFTSDNPR SEDPKQILRD 

       430        440        450        460        470        480 
MEAGVSAEIG KHVTIPDREE AIRYAIGQAQ EGDVVLIAGK GHETYQIIGN DVIEFDDRAV 


ARAAVKERG

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed: 15576355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000043 Genomic DNA. Translation: BAD75400.1.
RefSeqYP_146968.1. NC_006510.1.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
ProteinModelPortalQ5L0Y0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3186416.
GenomeReviewsGene locus GK1115 in contig BA000043_GR.
KEGGgka:GK1115.
NMPDRfig|235909.3.peg.2136.
PATRIC21963491. VBIGeoKau81518_1215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAGALAYVD.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycGKAU235909:GK1115-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_GEOKA
AccessionPrimary (citable) accession number: Q5L0Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 52 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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