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Q9AKI7 (MURE_RICRI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 70. 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
OrganismRickettsia rickettsii
Taxonomic identifier783 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length479 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 HAMAP-Rule MF_00208.

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 – 479479UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101935

Regions

Nucleotide binding98 – 1047ATP Potential
Region144 – 1452UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region396 – 3994Meso-diaminopimelate binding By similarity
Motif396 – 3994Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site211UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1711UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1791UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3721Meso-diaminopimelate By similarity
Binding site4461Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4501Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2111N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AKI7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: BE5379B53EC28326

FASTA47953,640
        10         20         30         40         50         60 
MSHNLKQLFQ QHNVKGLSIN SKTVKDKDIF FAIKGRNTDG NDFIKDALSK GAVLVITDNK 

        70         80         90        100        110        120 
KNIVIDKVIY VKDVQAALYE AIEIFYPKKP KDLIAVTGTN GKSSVVSYIA QTYSLLGKKA 

       130        140        150        160        170        180 
ASIGTIGVEI FGCVNLINDV PELTTLDYLS FRKIAHNLAE NGIEYLVFEA SSHGLDQARL 

       190        200        210        220        230        240 
REIKVNIACF TSFSQDHLDY HHTKENYLLA KLKLFINHLL PNGIAILNSD IEEIEFVKDY 

       250        260        270        280        290        300 
LHNHNVKFIT VGTKGDLEIT RLNCSLKGQN INFTFNNREY NFNTPIIGSF QASNLLIAVL 

       310        320        330        340        350        360 
SIHYIGFAFD DVIDSLVEVK AVKGRMERID NTNIFVDYAH TPDALEKALT ELKNIKLRDS 

       370        380        390        400        410        420 
KLSVVFGCGG NRDKAKRSLM GQIAAKRADT IIITDDNPRH EDPKLIRAEI ISGIEKADYT 

       430        440        450        460        470 
EIANREEAIK YGINNLKQDD ILLVAGKGHE NYQIIGDKKL PFDDAEVVRK CIKVCHPVA 

« Hide

References

[1]"Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes."
Andersson J.O., Andersson S.G.E.
Mol. Biol. Evol. 18:829-839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 84-21C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ293314 Genomic DNA. Translation: CAC33671.1.

3D structure databases

ProteinModelPortalQ9AKI7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.40.1390.10. 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. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
SSF63418. SSF63418. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_RICRI
AccessionPrimary (citable) accession number: Q9AKI7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways