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Q9Z8C5 (MURE_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 108. 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:CPn_0418, CP_0336, CpB0434
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

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 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 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101881

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
Q9Z8C5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 3A0FEEA93EDD76ED

FASTA48352,720
        10         20         30         40         50         60 
MDLKELLHGV QAKIYGKVRP LEVRNLTRDS RCVSVGDIFI AHKGQRYDGN DFAVDALANG 

        70         80         90        100        110        120 
AIAIASSLYN PFLSVVQIIT PNLEELEAEL SAKYYEYPSS KLHTIGVTGT NGKTTVTCLI 

       130        140        150        160        170        180 
KALLDSYQKP SGLLGTIEHI LGEGVIKDGF TTPTPALLQK YLATMVRQNR DAVVMEVSSI 

       190        200        210        220        230        240 
GLASGRVAYT NFDTAVLTNI TLDHLDFHGT FETYVAAKAK LFSLVPPSGM VVINTDSPYA 

       250        260        270        280        290        300 
SQCIESAKAP VITYGIESAA DYRATDIQLS SSGTKYTLVY GDQKIACSSS FIGKYNVYNL 

       310        320        330        340        350        360 
LAAISTVHAS LRCDLEDLLE KIGLCQPPPG RLDPVLMGPC PVYIDYAHTP DALDNVLTGL 

       370        380        390        400        410        420 
HELLPEGGRL IVVFGCGGDR DRSKRKLMAQ VVERYGFAVV TSDNPRSEPP EDIVNEICDG 

       430        440        450        460        470        480 
FYSKNYFIEI DRKQAITYAL SIASDRDIVL IAGKGHEAYQ IFKHQTVAFD DKQTVCEVLA 


SYV 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD18562.1.
AE002161 Genomic DNA. Translation: AAF38190.1.
BA000008 Genomic DNA. Translation: BAA98626.1.
AE009440 Genomic DNA. Translation: AAP98365.1.
PIRD72080.
H86542.
RefSeqNP_224618.1. NC_000922.1.
NP_300475.1. NC_002491.1.
NP_444885.1. NC_002179.2.
NP_876708.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z8C5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD18562; AAD18562; CPn_0418.
AAF38190; AAF38190; CP_0336.
AAP98365; AAP98365; CpB0434.
BAA98626; BAA98626; BAA98626.
GeneID1467115.
894904.
919161.
962867.
KEGGcpa:CP0336.
cpj:CPj0418.
cpn:CPn0418.
cpt:CpB0434.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAAVMTNLS.
OrthoDBEOG6PKFCR.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-349-MONOMER.
CPNE115713:GHEY-434-MONOMER.
CPNE138677:GH8N-429-MONOMER.
CPNE182082:GH4N-446-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_CHLPN
AccessionPrimary (citable) accession number: Q9Z8C5
Secondary accession number(s): Q9JQA1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 108 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