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Reviewed, UniProtKB/Swiss-Prot Q8X9Z2 (MURE_ECO57)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase
Gene names
Name: murE
Ordered Locus Names: Z0095, ECs0089
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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.

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.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity.

Sequence similarities

Belongs to the murCDEF family. MurE subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 495494UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101895

Regions

Nucleotide binding116 – 1227ATP Potential
Region44 – 463UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region158 – 1592UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region414 – 4174Meso-diaminopimelate binding By similarity
Motif414 – 4174Meso-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 site3901Meso-diaminopimelate By similarity
Binding site4651Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4691Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2251N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8X9Z2-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 17BEAB408DCF1BEB

FASTA49553,390
        10         20         30         40         50         60 
MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR YIPQAIAQGV 

        70         80         90        100        110        120 
AAIIAEAKGE ATDGEIREMH GVPVIYLSQL NERLSALAGR FYHEPSDNLR LVGVTGTNGK 

       130        140        150        160        170        180 
TTTTQLLAQW SQLLGETSAV MGTVGNGLLG KVIPTENTTG SAVDVQHELA GLVDQDATFC 

       190        200        210        220        230        240 
AMEVSSHGLV QHRVAALKFA ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN 

       250        260        270        280        290        300 
ADDEVGRRWL AKLPDAVAVS MEDHINPNCH GRWLKATEVN YHDSGATIRF SSSWGDGEIE 

       310        320        330        340        350        360 
SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG KPTVVVDYAH 

       370        380        390        400        410        420 
TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA IAEEFADVAV VTDDNPRTEE 

       430        440        450        460        470        480 
PRAIINDILA GMLDAGHAKV MEDRAEAVTC AVMQAKENDV VLVAGKGHED YQIVGNQRLD 

       490 
YSDRVTVARL LGVIA

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References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

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Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG54389.1.
BA000007 Genomic DNA. Translation: BAB33512.1.
PIRA85491.
A90640.
RefSeqNP_285781.1.
NP_308116.1.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
SMRQ8X9Z2. Positions 3-495.
ModBaseSearch...

Genome annotation databases

GeneID913536.
956771.
GenomeReviewsGene locus Z0095 in contig AE005174_GR.
Gene locus ECs0089 in contig BA000007_GR.
KEGGece:Z0095.
ecs:ECs0089.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8X9Z2.

Enzyme and pathway databases

BioCycECOL83334:ECS0089-MON.

Family and domain databases

HAMAPMF_00208.
[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]
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameMURE_ECO57
AccessionPrimary (citable) accession number: Q8X9Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 55 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents