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Protein

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

Gene

murE

Organism
Shigella flexneri
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 sitei27UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygenUniRule annotation1
Binding sitei29UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei157UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei185UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei191UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei193UDP-MurNAc-L-Ala-D-GluUniRule annotation1
Binding sitei390Meso-diaminopimelateUniRule annotation1
Binding sitei465Meso-diaminopimelate; via carbonyl oxygenUniRule annotation1
Binding sitei469Meso-diaminopimelateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi116 – 122ATPUniRule annotation7

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

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:SF0082, S0084
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 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_00001019391 – 495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseAdd BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei225N6-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

PaxDbiQ83MG0.
PRIDEiQ83MG0.

Interactioni

Protein-protein interaction databases

STRINGi198214.SF0082.

Structurei

3D structure databases

ProteinModelPortaliQ83MG0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 46UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation3
Regioni158 – 159UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation2
Regioni414 – 417Meso-diaminopimelate bindingUniRule annotation4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi414 – 417Meso-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.

Q83MG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR
60 70 80 90 100
YIPQAIAQGV AAIIAEAKDE ATDGEIREMH GVPVIYLSQL NERLSALAGR
110 120 130 140 150
FYHEPSDNLR LVGVTGTNGK TTTTQLLAQW SQLLGETSAV MGTVGNGLLG
160 170 180 190 200
KVIPTENTTG SAVDVQHELA GLVDQGATFC AMEVSSHGLV QHRVAALKFP
210 220 230 240 250
ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN ADDEVGRRWL
260 270 280 290 300
AKLPDAVAVS MEDHINPNCH GRWLKATEVN YHDSGATIRF SSSWGDGEIE
310 320 330 340 350
SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG
360 370 380 390 400
KPTVVVDYAH TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA
410 420 430 440 450
IAEEFADVAV VTDDNPRTEE PRAIINDILA GMLDAGHAKV MEGRAEAVTC
460 470 480 490
AVMQAKENDV VLVAGKGHED YQIVGNQRLD YSDRVTVARL LGGIA
Length:495
Mass (Da):53,315
Last modified:June 1, 2003 - v1
Checksum:iF070E7ECF0907A9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN41747.1.
AE014073 Genomic DNA. Translation: AAP15628.1.
RefSeqiNP_706040.1. NC_004337.2.
WP_000785134.1. NZ_LVJC01000012.1.

Genome annotation databases

EnsemblBacteriaiAAN41747; AAN41747; SF0082.
AAP15628; AAP15628; S0084.
GeneIDi1024503.
KEGGisfl:SF0082.
sft:NCTC1_00083.
sfx:S0084.
PATRICi18701108. VBIShiFle31049_0096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN41747.1.
AE014073 Genomic DNA. Translation: AAP15628.1.
RefSeqiNP_706040.1. NC_004337.2.
WP_000785134.1. NZ_LVJC01000012.1.

3D structure databases

ProteinModelPortaliQ83MG0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF0082.

Proteomic databases

PaxDbiQ83MG0.
PRIDEiQ83MG0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN41747; AAN41747; SF0082.
AAP15628; AAP15628; S0084.
GeneIDi1024503.
KEGGisfl:SF0082.
sft:NCTC1_00083.
sfx:S0084.
PATRICi18701108. VBIShiFle31049_0096.

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_SHIFL
AccessioniPrimary (citable) accession number: Q83MG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 98 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

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.