Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q823N2 (MURE_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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:CCA_00376
OrganismChlamydophila caviae [Complete proteome] [HAMAP]
Taxonomic identifier83557 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length483 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 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 MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208

Subcellular location

Cytoplasm By similarity HAMAP MF_00208.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101879

Regions

Nucleotide binding109 – 1157ATP Potential
Region151 – 1522UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region403 – 4064Meso-diaminopimelate binding By similarity
Motif403 – 4064Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1781UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3801Meso-diaminopimelate By similarity
Binding site4531Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4571Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q823N2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7360E8240C551A4D

FASTA48353,175
        10         20         30         40         50         60 
MNLKELLNNI EAKIYGKVSP IEVRNLTKDS RNVGFGDIFI ANKGKQFDGN DFSPLAIENG 

        70         80         90        100        110        120 
AIAIASSIYN PFLSVVQIVS SNLPQLEAEL SAKYYNYPSK KLCIVGVTGT NGKTTVSHLI 

       130        140        150        160        170        180 
KTLFDGCNKP SGLIGTIEHV LGNNRIQDGY TTPESCLLQK YLAEMVKNRL TSAVMEVSSV 

       190        200        210        220        230        240 
GLVLERLAEV DFDVGVLTNI TLDHLDFHGS FEEYINAKLK LFSKLPATGL AVVNGDLSYA 

       250        260        270        280        290        300 
SRFLEMTQAQ PITYGIECPA DYRAMHLRSS PFGTDFDLVY RGESLPCRLP LIGKHNVYNI 

       310        320        330        340        350        360 
LAAIAVAHQH CNGDLQQLIS LAANVESPRG RLEPVFSGPC PIYIDYAHTP DALENVCKTL 

       370        380        390        400        410        420 
HALLPEQGKL IVVFGCGGDR DQSKRQIMAE VVERYGFAVV TSDNPRGEDP EEIIKAICSG 

       430        440        450        460        470        480 
FVKRNFSIEI DRKQAITYAL SIASDRDIVL VAGKGHETYQ IFKHQTIAFD DKEIVREVLS 


SHV 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05123.1.
RefSeqNP_829245.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ823N2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1218061.
GenomeReviewsGene locus CCA_00376 in contig AE015925_GR.
KEGGcca:CCA00376.
PATRIC20269814. VBIChlCav107360_0405.
TIGRCCA_00376.

Phylogenomic databases

HOGENOMHBG602753.
OMAHTTPEST.
PhylomeDBQ823N2.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCCAV227941:CCA_00376-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[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.
KOK01928.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. MurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_CHLCV
AccessionPrimary (citable) accession number: Q823N2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families