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Q9PKC6 (MURE_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. 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:TC_0540
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [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 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_0000101880

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
Q9PKC6 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: E459FA97D45D17D4

FASTA48352,941
        10         20         30         40         50         60 
MHLDQLLRDI PAKIYGKVES IPVRNLTRDS RCTGVGDIFI ARQGQMCNGN DYSGQAVENG 

        70         80         90        100        110        120 
AIAILSSLYN PFLSVVQIVT EDLTALEACL AARFYNDPSK RLDVIGVTGT NGKTTVSALA 

       130        140        150        160        170        180 
RELMEYKGRC TGLVGTIEHI LGEHRIIDSF TTPDAILLQK YFAEMVKQNL SSAVVEVSSI 

       190        200        210        220        230        240 
GLALGRVRET EFLAGVLTNV SLDHLDFHGS FEEYVVAKKQ LFVSLPEHGV AVVNSDCEYA 

       250        260        270        280        290        300 
QSFLEISPAR GVSYAVHQEA DYRAVNLKFS SLGSTFDILY QGNVFSCETS LVGEHNVYNV 

       310        320        330        340        350        360 
LAALSVVHQI LGGDFAELVH YVRYLSAPKG RLEPVLSGPC PIYIDYAHTP DALDNVCKIL 

       370        380        390        400        410        420 
SQLLPADGRL IIVFGCGGDR DHSKRPIMAK VAETYGFSVV TSDNPRTEDP DQIIADICSG 

       430        440        450        460        470        480 
FSTDRYVIES DRRLAIVKAI SMALDKDIVL VAGKGHEVYQ IFKHQTIVFD DREVVCEALA 


SIY

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002160 Genomic DNA. Translation: AAF39380.1.
PIRH81691.
RefSeqNP_296917.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PKC6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1245900.
GenomeReviewsGene locus TC_0540 in contig AE002160_GR.
KEGGcmu:TC0540.
PATRIC20372524. VBIChlMur19118_0578.
TIGRTC_0540.

Phylogenomic databases

HOGENOMHBG602753.
PhylomeDBQ9PKC6.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCMUR243161:TC_0540-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_CHLMU
AccessionPrimary (citable) accession number: Q9PKC6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 30, 2003
Last modified: January 25, 2012
This is version 82 of the entry and version 2 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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