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Q3KM93 (MURE_CHLTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. 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:CTA_0291
OrganismChlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP]
Taxonomic identifier315277 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia ›

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-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.

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 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012346

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-Rule 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
Q3KM93 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: AFD354C9E5F3FC95

FASTA48353,334
        10         20         30         40         50         60 
MHLDQLLQNI PAKIYGKVES IPVRNLTRDS RCVGVGDIFI ARQGQFCNGN DYSSQAVANG 

        70         80         90        100        110        120 
AIAVLSSLYN PFLSVVQIIA EDPIALEASL AARFYNNPSR HLDVIGITGT NGKTTVSCLV 

       130        140        150        160        170        180 
RELMERSGRR TGLIGTIEHI LGENRIIDSF TTPDAILLQK YFAEMVKQNL SAAVMEVSSI 

       190        200        210        220        230        240 
GMALGRVRET EFLAGVLTNI TSDHLDFHGS LEEYIAAKKQ FFASLPEKGI AVVNLDCEYA 

       250        260        270        280        290        300 
PSFLNGSQAR AVSYAIHQEA DYRADRLKLY SSGSSYDIWY QGQVFPCETS LIGEHNVYNV 

       310        320        330        340        350        360 
LASLAVVHQF LGRDFADLVR DVRFLSAPKG RLDPILLGPF PVYIDYAHTP DALDNVCRIL 

       370        380        390        400        410        420 
LQLLPKDGRL IIVFGCGGDR DRVKRPLMAK VSEHYGFSFV TSDNPRTEDP DQIIADICKG 

       430        440        450        460        470        480 
FSTDHYVVES DRKLAIEKAI SMASDKDIVL VAGKGHEGYQ IFKHQTIVFD DREVVCEALA 


ALC

« Hide

References

[1]"Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains."
Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.
Infect. Immun. 73:6407-6418(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAR-13 / ATCC VR-571B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000051 Genomic DNA. Translation: AAX50529.1.
RefSeqYP_328077.1. NC_007429.1.

3D structure databases

ProteinModelPortalQ3KM93.
ModBaseSearch...

Protein-protein interaction databases

STRING315277.CTA_0291.

Proteomic databases

PRIDEQ3KM93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX50529; AAX50529; CTA_0291.
GeneID3687321.
KEGGcta:CTA_0291.
PATRIC32022460. VBIChlTra31516_0300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMARPLMGEA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCTRA315277:GI4C-329-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 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. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_CHLTA
AccessionPrimary (citable) accession number: Q3KM93
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: May 1, 2013
This is version 59 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

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