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A7Z4E1 (MURE_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. 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:RBAM_015040
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length490 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 – 490490UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012336

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
A7Z4E1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: DF23F229249AF110

FASTA49053,948
        10         20         30         40         50         60 
MKLTKLLTYL MAEPVQNDFH DPDITSIEMD SREVRKGSLF VCIKGYTVDG HDFAQKAAEN 

        70         80         90        100        110        120 
GAAAIVAEKE LDVDVPVIIV RRSQRALSVL SDAFYGQPTK QLQLIGITGT NGKTSTTHMV 

       130        140        150        160        170        180 
DEIFKKAGRQ TGLIGTMYIK IGDETFPVKN TTPESVTLQK TFKKMNDEHV DTAIMEVSSH 

       190        200        210        220        230        240 
ALSLGRVHGC DYDIAVFTNL TQDHLDYHKT MEDYRQAKSL LFSQLGGSFN HEKPKRAVLN 

       250        260        270        280        290        300 
ADDKASAYFE KVTAAHILTY GIENDADVMA KQIEISAQGT SFELVTPKGT KQITVSLVGR 

       310        320        330        340        350        360 
FNVYNVLAAA ATGIAAGLPF DTITSALEEL QGVRGRFELV NHNQPFPVVV DYAHTPDSLE 

       370        380        390        400        410        420 
NVLNTCKDMT EGKLFVVVGC GGDRDKTKRP KMAEIAVRIA DEPIFTSDNP RSEDPLAILR 

       430        440        450        460        470        480 
DMERGVEGTY YHSIANREQA IFFAIANAKK GDVVLIAGKG HETYQQIGNE TFDFDDAEVA 

       490 
GRAIVELNKK

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References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000560 Genomic DNA. Translation: ABS73867.1.
RefSeqYP_001421098.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z4E1.
ModBaseSearch...

Protein-protein interaction databases

STRING326423.RBAM_015040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS73867; ABS73867; RBAM_015040.
GeneID5461794.
KEGGbay:RBAM_015040.
PATRIC18748066. VBIBacAmy31356_1509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

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_BACA2
AccessionPrimary (citable) accession number: A7Z4E1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: May 1, 2013
This is version 49 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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