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Q9A595 (MURE_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:CC_2559
OrganismCaulobacter crescentus (Caulobacter vibrioides)
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length486 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 – 486486UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101878

Regions

Nucleotide binding104 – 1107ATP Potential
Region152 – 1532UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region407 – 4104Meso-diaminopimelate binding By similarity
Motif407 – 4104Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site261UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1791UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1871UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3831Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9A595 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0BDA4EFDE8A1C016

FASTA48649,992
        10         20         30         40         50         60 
MTKRLSDLFN RPFATDPVIA GVTADSRKVT TGWLFAALPG TKVDGRDFAE GAVAKGAAAI 

        70         80         90        100        110        120 
LAPEGGLEGL GVPVVRSEDA RRAYALAAAA FWGKQPAMCV AVTGTNGKTS VAGFCRQIFT 

       130        140        150        160        170        180 
KLGHKAASMG TLGVVVSQPG QPDQQLTPPG LTTPDAGDVA EMIARLADMG VTHLALEASS 

       190        200        210        220        230        240 
HGVDQRRIDG VKLSAAGFTN FTQDHLDYHG SMEAYRAAKL RLFDTLTPAG AMAVLNADSE 

       250        260        270        280        290        300 
AFPDFAAAAV TSGQSVFSVG EEGQGLRLLS RTPTPAGQDL VVEAEGVVHH LKLPLAGAFQ 

       310        320        330        340        350        360 
ASNVLVAAGL CIAAGEDSAK VLKALETLEG AAGRLQRVGR GPKGGEAYVD YAHTPDGLQT 

       370        380        390        400        410        420 
VLEALRPHTA GKLIAVFGAG GDRDRGKRPL MGAIGAKLAD IAIVTDDNPR SEDPASIRAA 

       430        440        450        460        470        480 
ILEAAPGARE IGDRRAAIRA AVALMSEGDV LVVAGKGHEQ GQIVAGVVHP FDDVAETLQA 


LEGVDA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK24529.1.
PIRE87566.
RefSeqNP_421361.1. NC_002696.2.

3D structure databases

ProteinModelPortalQ9A595.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID942512.
GenomeReviewsGene locus CC_2559 in contig AE005673_GR.
KEGGccr:CC_2559.
NMPDRfig|190650.1.peg.2541.
PATRIC21302144. VBICauCre124313_2573.
TIGRCC_2559.

Phylogenomic databases

HOGENOMHBG602753.
OMAHTTPEST.
ProtClustDBPRK00139.

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_CAUCR
AccessionPrimary (citable) accession number: Q9A595
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 74 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