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Protein

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

Gene

murE

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathway:ipeptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei178 – 1781UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei186 – 1861UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei380 – 3801Meso-diaminopimelateUniRule annotation
Binding sitei453 – 4531Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
Binding sitei457 – 4571Meso-diaminopimelateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1157ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciCPNE115711:GI7B-349-MONOMER.
CPNE115713:GHEY-434-MONOMER.
CPNE138677:GH8N-429-MONOMER.
CPNE182082:GH4N-446-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseUniRule annotation (EC:6.3.2.13UniRule annotation)
Alternative name(s):
Meso-A2pm-adding enzymeUniRule annotation
Meso-diaminopimelate-adding enzymeUniRule annotation
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligaseUniRule annotation
UDP-MurNAc-tripeptide synthetaseUniRule annotation
UDP-N-acetylmuramyl-tripeptide synthetaseUniRule annotation
Gene namesi
Name:murEUniRule annotation
Ordered Locus Names:CPn_0418, CP_0336, CpB0434
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000583 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181N6-carboxylysineUniRule annotation

Post-translational modificationi

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.UniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi115713.CPn0418.

Structurei

3D structure databases

ProteinModelPortaliQ9Z8C5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1522UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
Regioni403 – 4064Meso-diaminopimelate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi403 – 4064Meso-diaminopimelate recognition motif

Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiVDYAHTG.
OrthoDBiEOG6PKFCR.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.40.1390.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPiMF_00208. MurE.
InterProiIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
PfamiPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
SSF63418. SSF63418. 1 hit.
TIGRFAMsiTIGR01085. murE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z8C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLKELLHGV QAKIYGKVRP LEVRNLTRDS RCVSVGDIFI AHKGQRYDGN
60 70 80 90 100
DFAVDALANG AIAIASSLYN PFLSVVQIIT PNLEELEAEL SAKYYEYPSS
110 120 130 140 150
KLHTIGVTGT NGKTTVTCLI KALLDSYQKP SGLLGTIEHI LGEGVIKDGF
160 170 180 190 200
TTPTPALLQK YLATMVRQNR DAVVMEVSSI GLASGRVAYT NFDTAVLTNI
210 220 230 240 250
TLDHLDFHGT FETYVAAKAK LFSLVPPSGM VVINTDSPYA SQCIESAKAP
260 270 280 290 300
VITYGIESAA DYRATDIQLS SSGTKYTLVY GDQKIACSSS FIGKYNVYNL
310 320 330 340 350
LAAISTVHAS LRCDLEDLLE KIGLCQPPPG RLDPVLMGPC PVYIDYAHTP
360 370 380 390 400
DALDNVLTGL HELLPEGGRL IVVFGCGGDR DRSKRKLMAQ VVERYGFAVV
410 420 430 440 450
TSDNPRSEPP EDIVNEICDG FYSKNYFIEI DRKQAITYAL SIASDRDIVL
460 470 480
IAGKGHEAYQ IFKHQTVAFD DKQTVCEVLA SYV
Length:483
Mass (Da):52,720
Last modified:May 1, 1999 - v1
Checksum:i3A0FEEA93EDD76ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA. Translation: AAD18562.1.
AE002161 Genomic DNA. Translation: AAF38190.1.
BA000008 Genomic DNA. Translation: BAA98626.1.
AE009440 Genomic DNA. Translation: AAP98365.1.
PIRiD72080.
H86542.
RefSeqiNP_224618.1. NC_000922.1.

Genome annotation databases

EnsemblBacteriaiAAD18562; AAD18562; CPn_0418.
AAF38190; AAF38190; CP_0336.
AAP98365; AAP98365; CpB0434.
BAA98626; BAA98626; BAA98626.
GeneIDi894904.
KEGGicpa:CP0336.
cpj:CPj0418.
cpn:CPn0418.
cpt:CpB0434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA. Translation: AAD18562.1.
AE002161 Genomic DNA. Translation: AAF38190.1.
BA000008 Genomic DNA. Translation: BAA98626.1.
AE009440 Genomic DNA. Translation: AAP98365.1.
PIRiD72080.
H86542.
RefSeqiNP_224618.1. NC_000922.1.

3D structure databases

ProteinModelPortaliQ9Z8C5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi115713.CPn0418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD18562; AAD18562; CPn_0418.
AAF38190; AAF38190; CP_0336.
AAP98365; AAP98365; CpB0434.
BAA98626; BAA98626; BAA98626.
GeneIDi894904.
KEGGicpa:CP0336.
cpj:CPj0418.
cpn:CPn0418.
cpt:CpB0434.

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiVDYAHTG.
OrthoDBiEOG6PKFCR.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciCPNE115711:GI7B-349-MONOMER.
CPNE115713:GHEY-434-MONOMER.
CPNE138677:GH8N-429-MONOMER.
CPNE182082:GH4N-446-MONOMER.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.40.1390.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPiMF_00208. MurE.
InterProiIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
PfamiPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
SSF63418. SSF63418. 1 hit.
TIGRFAMsiTIGR01085. murE. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CWL029.
  2. 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.

Entry informationi

Entry nameiMURE_CHLPN
AccessioniPrimary (citable) accession number: Q9Z8C5
Secondary accession number(s): Q9JQA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.