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Q83F28 (MURE_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:CBU_0123
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length489 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 – 489489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101891

Regions

Nucleotide binding113 – 1197ATP Potential
Region155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region412 – 4154Meso-diaminopimelate binding By similarity
Motif412 – 4154Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3881Meso-diaminopimelate By similarity
Binding site4631Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4671Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83F28 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6AC4716157215B22

FASTA48953,828
        10         20         30         40         50         60 
MNGKYLSQLL DAKNKALTAD VLIKALQTDS RKIQPGDLFI AYPGLQVDGR DYIKEALDKK 

        70         80         90        100        110        120 
AAAVFYEANQ YNPSIQTKVP LIPFENLQHR IGEIAARFYD DPSCEMEIIG ITGTNGKTSC 

       130        140        150        160        170        180 
AQFIAQALQS QGIRCGVIGT LGYGFLGSLH KTSHTTPEPI QLQQAFAEMR KQGAKAIAME 

       190        200        210        220        230        240 
VSSHALHQRR VEGVQFDIAV FTQLSRDHLD YHGDMENYAR AKELLFQQPG LHTGVVNCDD 

       250        260        270        280        290        300 
ALGKRIIAHY RHQLTLVGYS ANGVKDDRVS SVIASAIQPL AQGFSVEVQT PWGEGTFTTP 

       310        320        330        340        350        360 
LFGRFNISNL LAVLSVLCLC EIPFDKALLE LSQLRNVPGR MQVVDSQRQP QIIVDYAHTP 

       370        380        390        400        410        420 
DALEKALTAL REHCQGRLIC VFGCGGDRDR GKRPQMAAVA EQHADQIILT NDNPRTESPL 

       430        440        450        460        470        480 
TIIQDIQAGF KNKNAVLVKL DRAEAIRYAV QMAAVNDIVL IAGKGHETTQ TIADQVLPFN 


DVEEAKKAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO89687.1.
RefSeqNP_819173.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83F28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_0123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO89687; AAO89687; CBU_0123.
GeneID1207994.
KEGGcbu:CBU_0123.
PATRIC17928931. VBICoxBur82552_0126.

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAKIKMIGN.
OrthoDBEOG6PKFCR.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-128-MONOMER.
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_COXBU
AccessionPrimary (citable) accession number: Q83F28
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: March 19, 2014
This is version 77 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names