Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9ZJC6 (MURE_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:jhp_1387
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length447 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 – 447447UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101903

Regions

Nucleotide binding74 – 807ATP Potential
Region117 – 1182UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region364 – 3674Meso-diaminopimelate binding By similarity
Motif364 – 3674Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site211UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1441UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1501UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1521UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3401Meso-diaminopimelate By similarity
Binding site4151Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4191Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue1841N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZJC6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 639AB9D18F3740BD

FASTA44750,660
        10         20         30         40         50         60 
MKLKKTLTYQ HHAYSFLSDN TNEVLENPKE ILFVKTPLNE KYAPLIAEKN LAILDFNELK 

        70         80         90        100        110        120 
NYFDFKIKIV GITGTNGKTT TASLMYSLLL DLNKKTALLG TRGFFIDDKH IKEKGLTTPT 

       130        140        150        160        170        180 
LLELYSDLEE AIRLKCEYFI MEVSSHAIVQ KRIAGLDFAL KILTNITSDH LDFHQNIENY 

       190        200        210        220        230        240 
RDAKNSFFKD EGLKVINRDE TNALFNPINA RTYALDKKAH LNVQAFSLNP SISASLCYQH 

       250        260        270        280        290        300 
DLRDPNLKET ALIHSPLLGR YNLYNILAGV LGVKLLTQLP LETIAPLLEN FYGVKGRLEI 

       310        320        330        340        350        360 
VHSKPLVVVD FAHTTDGMQQ VFESFKNQKI TALFGAGGDR DKTKRPKMGA IASCYAHQII 

       370        380        390        400        410        420 
LTSDNPRSEN EEDIIKDILK GINNSSKVIV EKDRKKAILN ALENLKDDEV LLILGKGDEN 

       430        440 
IQIFKDKTIF FSDQEVVKDY YLNLKQG 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06968.1.
PIRD71812.
RefSeqNP_224105.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZJC6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp1387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06968; AAD06968; jhp_1387.
GeneID889938.
KEGGhpj:jhp1387.
PATRIC20607654. VBIHelPyl98156_1506.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
KOK01928.
OMAAVMTNLS.
OrthoDBEOG6PKFCR.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-1426-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
PfamPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_HELPJ
AccessionPrimary (citable) accession number: Q9ZJC6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 104 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