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Protein

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

Gene

murE

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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

Pathwayi: peptidoglycan 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)DescriptionActionsGraphical viewLength
Binding sitei30UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei182UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei188UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei190UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei388Meso-diaminopimelateUniRule annotation1
Binding sitei463Meso-diaminopimelate; via carbonyl oxygenUniRule annotation1
Binding sitei467Meso-diaminopimelateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi113 – 119ATPUniRule annotation7

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: TIGR
  • regulation of cell shape Source: UniProtKB-KW
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

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:CBU_0123
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001018911 – 489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseAdd BLAST489

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei222N6-carboxylysineUniRule annotation1

Post-translational modificationi

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

Proteomic databases

PRIDEiQ83F28.

Interactioni

Protein-protein interaction databases

STRINGi227377.CBU_0123.

Structurei

3D structure databases

ProteinModelPortaliQ83F28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni155 – 156UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation2
Regioni412 – 415Meso-diaminopimelate bindingUniRule annotation4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi412 – 415Meso-diaminopimelate recognition motif4

Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107EEN. Bacteria.
COG0769. LUCA.
HOGENOMiHOG000268118.
KOiK01928.
OMAiHNHNIKF.

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. 1 hit.
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.

Q83F28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGKYLSQLL DAKNKALTAD VLIKALQTDS RKIQPGDLFI AYPGLQVDGR
60 70 80 90 100
DYIKEALDKK AAAVFYEANQ YNPSIQTKVP LIPFENLQHR IGEIAARFYD
110 120 130 140 150
DPSCEMEIIG ITGTNGKTSC AQFIAQALQS QGIRCGVIGT LGYGFLGSLH
160 170 180 190 200
KTSHTTPEPI QLQQAFAEMR KQGAKAIAME VSSHALHQRR VEGVQFDIAV
210 220 230 240 250
FTQLSRDHLD YHGDMENYAR AKELLFQQPG LHTGVVNCDD ALGKRIIAHY
260 270 280 290 300
RHQLTLVGYS ANGVKDDRVS SVIASAIQPL AQGFSVEVQT PWGEGTFTTP
310 320 330 340 350
LFGRFNISNL LAVLSVLCLC EIPFDKALLE LSQLRNVPGR MQVVDSQRQP
360 370 380 390 400
QIIVDYAHTP DALEKALTAL REHCQGRLIC VFGCGGDRDR GKRPQMAAVA
410 420 430 440 450
EQHADQIILT NDNPRTESPL TIIQDIQAGF KNKNAVLVKL DRAEAIRYAV
460 470 480
QMAAVNDIVL IAGKGHETTQ TIADQVLPFN DVEEAKKAL
Length:489
Mass (Da):53,828
Last modified:June 1, 2003 - v1
Checksum:i6AC4716157215B22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO89687.1.
RefSeqiNP_819173.1. NC_002971.3.
WP_005769454.1. NZ_CCYB01000063.1.

Genome annotation databases

EnsemblBacteriaiAAO89687; AAO89687; CBU_0123.
GeneIDi1207994.
KEGGicbu:CBU_0123.
PATRICi17928931. VBICoxBur82552_0126.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO89687.1.
RefSeqiNP_819173.1. NC_002971.3.
WP_005769454.1. NZ_CCYB01000063.1.

3D structure databases

ProteinModelPortaliQ83F28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_0123.

Proteomic databases

PRIDEiQ83F28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO89687; AAO89687; CBU_0123.
GeneIDi1207994.
KEGGicbu:CBU_0123.
PATRICi17928931. VBICoxBur82552_0126.

Phylogenomic databases

eggNOGiENOG4107EEN. Bacteria.
COG0769. LUCA.
HOGENOMiHOG000268118.
KOiK01928.
OMAiHNHNIKF.

Enzyme and pathway databases

UniPathwayiUPA00219.

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. 1 hit.
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...

Entry informationi

Entry nameiMURE_COXBU
AccessioniPrimary (citable) accession number: Q83F28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 91 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, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.