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O26027 (MURE_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HP_1494
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [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_0000101902

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
O26027 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 296349E8FE90AD34

FASTA44750,858
        10         20         30         40         50         60 
MKLKKTLTYQ NHTYSFLSDN THEVLENPKE ILFVKTPLNE KYSHLIAEKN LAILDFNELK 

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

       130        140        150        160        170        180 
LLELYSDLEE AVRLKCEYFI MEVSSHAIVQ KRIAGLDFAL KILTNITSDH LDFHQSIENY 

       190        200        210        220        230        240 
RDAKNSFFKD EGLKVINRDE TNALFNPVNA HTYALDKKAH LNVQAFSLNP SISASLCYQQ 

       250        260        270        280        290        300 
DLRDPNFKEI ALMHSPLLGR YNLYNILAGV LGVKLLTQLP LETIVPLLEN FYGVKGRLEI 

       310        320        330        340        350        360 
VHSKPLVVVD FAHTIDGMQQ VFESFKNQKI TALFGAGGDR DKTKRPEMGA IASYYAHKII 

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

       430        440 
IQIFKDKTIF FSDQEVVKSY YQHLKQG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD08535.1.
PIRF64706.
RefSeqNP_208285.1. NC_000915.1.
YP_006935420.1. NC_018939.1.

3D structure databases

ProteinModelPortalO26027.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO26027. 1 interaction.
STRING85962.HP1494.

Proteomic databases

PRIDEO26027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD08535; AAD08535; HP_1494.
GeneID899798.
KEGGheo:C694_07740.
hpy:HP1494.
PATRIC20594399. VBIHelPyl33062_1568.

Phylogenomic databases

eggNOGCOG0769.
KOK01928.
OMAGMIASEW.
OrthoDBEOG6PKFCR.

Enzyme and pathway databases

BioCycHPY:HP1494-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_HELPY
AccessionPrimary (citable) accession number: O26027
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 105 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

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names