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Reviewed, UniProtKB/Swiss-Prot Q253Y4 (MURE_CHLFF)

Last modified November 3, 2009. Version 29. 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

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: CF0632
OrganismChlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]
Taxonomic identifier264202 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydophila

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012344

Regions

Nucleotide binding111 – 1177ATP Potential
Region153 – 1542UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region405 – 4084Meso-diaminopimelate binding By similarity
Motif405 – 4084Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1801UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3821Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2201N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q253Y4-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 91A8312A531EFE64

FASTA48553,404
        10         20         30         40         50         60 
MNLKELLHNI DIDAKVYGKI SPIEVRNLTK DSRNIGFGDI FIANKGKRCD GNDFASLAVE 

        70         80         90        100        110        120 
NGAIAVVSSI YNPFLSVVQI ISPNLSLLEA QLAAKYYNYP SRKLCVVGIT GTNGKTTVSH 

       130        140        150        160        170        180 
LIKFLFDACD KPSGLIGTIE HILGNNRIQD GFTTPESCLL QKYLAEMVKS NLTAAVIETS 

       190        200        210        220        230        240 
SIGLVLDRLA NVEFDVGVLT NVTLDHLDFH DSFEEYIKAK LQLFAQLSDS GLAVVNNDLP 

       250        260        270        280        290        300 
QAKQFLEATR AVPVTYGIEQ LADYRASNLR FSPFGADFDL IHKGEIFPCH SPLIGQYNVY 

       310        320        330        340        350        360 
NVLAAIAVTH QRLNCDLQQL VSLVASVKSP RGRLEPIQSG PCPIYIDYAH TPDALDNVCQ 

       370        380        390        400        410        420 
TLRTLLPSGG KLIVVFGCGG DRDRSKRKIM AQVVEKYGFA VVTSDNPRGE DPETIVNEIC 

       430        440        450        460        470        480 
SGFVKRNFSI EIDRKQAITY ALSIASDRDI VLVAGKGHET YQIFKHQTIA FDDREVVHEV 


LSSYV 

« Hide

References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed: 16766509] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006861 Genomic DNA. Translation: BAE81404.1.
RefSeqYP_515549.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ253Y4.

Genome annotation databases

GeneID3958925.
GenomeReviewsGene locus CF0632 in contig AP006861_GR.
KEGGcfe:CF0632.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ253Y4.
OMAFPVIVDY.

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...

Entry information

Entry nameMURE_CHLFF
AccessionPrimary (citable) accession number: Q253Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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