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Protein

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

Gene

murE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine.3 Publications

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.2 Publications

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Activated by potassium phosphate.1 Publication

Kineticsi

  1. KM=76 µM for UDP-N-acetylmuramoyl-L-Ala-D-Glu2 Publications
  2. KM=36 µM for meso-diaminopimelate2 Publications
  3. KM=1500 µM for meso-lanthionine2 Publications
  4. KM=3900 µM for L-allo-cystathionine2 Publications
  5. KM=10000 µM for D-allo-cystathionine2 Publications
  6. KM=620 µM for ATP2 Publications
  1. Vmax=32 nmol/min/mg enzyme with meso-diaminopimelate as substrate2 Publications
  2. Vmax=23 nmol/min/mg enzyme with meso-lanthionine as substrate2 Publications
  3. Vmax=19 nmol/min/mg enzyme with L-allo-cystathionine as substrate2 Publications
  4. Vmax=23 nmol/min/mg enzyme with L-allo-cystathionine as substrate2 Publications

pH dependencei

Optimum pH is about 8.1 Publication

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
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 oxygen1
Binding sitei29UDP-MurNAc-L-Ala-D-Glu1
Binding sitei157UDP-MurNAc-L-Ala-D-Glu1
Binding sitei185UDP-MurNAc-L-Ala-D-Glu1
Binding sitei191UDP-MurNAc-L-Ala-D-Glu1
Binding sitei193UDP-MurNAc-L-Ala-D-Glu1
Binding sitei390Meso-diaminopimelate1
Binding sitei465Meso-diaminopimelate; via carbonyl oxygen1
Binding sitei469Meso-diaminopimelate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi116 – 122ATPSequence analysis7

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: EcoCyc
  • 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

BioCyciEcoCyc:UDP-NACMURALGLDAPLIG-MONOMER.
ECOL316407:JW0083-MONOMER.
MetaCyc:UDP-NACMURALGLDAPLIG-MONOMER.
BRENDAi6.3.2.13. 2026.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC:6.3.2.132 Publications)
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 namesi
Name:murE
Ordered Locus Names:b0085, JW0083
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10621. murE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3309032.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001018932 – 495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei225N6-carboxylysine1 Publication1

Post-translational modificationi

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.1 Publication

Proteomic databases

EPDiP22188.
PaxDbiP22188.
PRIDEiP22188.

2D gel databases

SWISS-2DPAGEP22188.

Interactioni

Protein-protein interaction databases

BioGridi4261641. 527 interactors.
DIPiDIP-10280N.
IntActiP22188. 20 interactors.
MINTiMINT-1230964.
STRINGi511145.b0085.

Chemistry databases

BindingDBiP22188.

Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 10Combined sources5
Turni11 – 13Combined sources3
Beta strandi25 – 27Combined sources3
Helixi29 – 31Combined sources3
Beta strandi37 – 40Combined sources4
Helixi48 – 51Combined sources4
Helixi52 – 57Combined sources6
Beta strandi61 – 66Combined sources6
Turni68 – 70Combined sources3
Beta strandi76 – 79Combined sources4
Beta strandi82 – 87Combined sources6
Helixi90 – 101Combined sources12
Helixi105 – 107Combined sources3
Beta strandi108 – 118Combined sources11
Helixi120 – 133Combined sources14
Beta strandi138 – 142Combined sources5
Beta strandi145 – 148Combined sources4
Beta strandi156 – 159Combined sources4
Helixi162 – 174Combined sources13
Beta strandi179 – 183Combined sources5
Helixi186 – 190Combined sources5
Turni191 – 196Combined sources6
Beta strandi200 – 204Combined sources5
Helixi212 – 215Combined sources4
Helixi218 – 230Combined sources13
Beta strandi236 – 240Combined sources5
Helixi244 – 250Combined sources7
Beta strandi257 – 263Combined sources7
Turni267 – 269Combined sources3
Beta strandi271 – 281Combined sources11
Beta strandi286 – 292Combined sources7
Beta strandi297 – 301Combined sources5
Helixi306 – 321Combined sources16
Helixi326 – 332Combined sources7
Helixi333 – 335Combined sources3
Beta strandi342 – 346Combined sources5
Beta strandi353 – 357Combined sources5
Helixi362 – 374Combined sources13
Beta strandi380 – 384Combined sources5
Beta strandi388 – 390Combined sources3
Helixi394 – 405Combined sources12
Beta strandi407 – 411Combined sources5
Helixi421 – 429Combined sources9
Helixi435 – 437Combined sources3
Beta strandi438 – 440Combined sources3
Helixi444 – 454Combined sources11
Beta strandi460 – 465Combined sources6
Beta strandi471 – 474Combined sources4
Beta strandi477 – 480Combined sources4
Helixi483 – 491Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E8CX-ray2.00A/B2-495[»]
ProteinModelPortaliP22188.
SMRiP22188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22188.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 46UDP-MurNAc-L-Ala-D-Glu binding3
Regioni158 – 159UDP-MurNAc-L-Ala-D-Glu binding2
Regioni414 – 417Meso-diaminopimelate binding4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi414 – 417Meso-diaminopimelate recognition motif4

Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.Curated

Phylogenomic databases

eggNOGiENOG4107EEN. Bacteria.
COG0769. LUCA.
HOGENOMiHOG000268118.
InParanoidiP22188.
KOiK01928.
OMAiHNHNIKF.
PhylomeDBiP22188.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22188-1 [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 SQLLGEISAV MGTVGNGLLG
160 170 180 190 200
KVIPTENTTG SAVDVQHELA GLVDQGATFC AMEVSSHGLV QHRVAALKFA
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 LGVIA
Length:495
Mass (Da):53,344
Last modified:January 23, 2007 - v2
Checksum:iD4A7A3E56D6C7E49
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti344E → K in murE1. 1
Natural varianti495A → S in murE1. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55814 Genomic DNA. Translation: CAA39334.1.
X55034 Genomic DNA. Translation: CAA38862.1.
U00096 Genomic DNA. Translation: AAC73196.1.
AP009048 Genomic DNA. Translation: BAB96653.1.
U67894 Genomic DNA. Translation: AAB60789.1.
PIRiS14384.
RefSeqiNP_414627.1. NC_000913.3.
WP_000775093.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73196; AAC73196; b0085.
BAB96653; BAB96653; BAB96653.
GeneIDi944791.
KEGGiecj:JW0083.
eco:b0085.
PATRICi32115275. VBIEscCol129921_0089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55814 Genomic DNA. Translation: CAA39334.1.
X55034 Genomic DNA. Translation: CAA38862.1.
U00096 Genomic DNA. Translation: AAC73196.1.
AP009048 Genomic DNA. Translation: BAB96653.1.
U67894 Genomic DNA. Translation: AAB60789.1.
PIRiS14384.
RefSeqiNP_414627.1. NC_000913.3.
WP_000775093.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E8CX-ray2.00A/B2-495[»]
ProteinModelPortaliP22188.
SMRiP22188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261641. 527 interactors.
DIPiDIP-10280N.
IntActiP22188. 20 interactors.
MINTiMINT-1230964.
STRINGi511145.b0085.

Chemistry databases

BindingDBiP22188.
ChEMBLiCHEMBL3309032.

2D gel databases

SWISS-2DPAGEP22188.

Proteomic databases

EPDiP22188.
PaxDbiP22188.
PRIDEiP22188.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73196; AAC73196; b0085.
BAB96653; BAB96653; BAB96653.
GeneIDi944791.
KEGGiecj:JW0083.
eco:b0085.
PATRICi32115275. VBIEscCol129921_0089.

Organism-specific databases

EchoBASEiEB0616.
EcoGeneiEG10621. murE.

Phylogenomic databases

eggNOGiENOG4107EEN. Bacteria.
COG0769. LUCA.
HOGENOMiHOG000268118.
InParanoidiP22188.
KOiK01928.
OMAiHNHNIKF.
PhylomeDBiP22188.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEcoCyc:UDP-NACMURALGLDAPLIG-MONOMER.
ECOL316407:JW0083-MONOMER.
MetaCyc:UDP-NACMURALGLDAPLIG-MONOMER.
BRENDAi6.3.2.13. 2026.

Miscellaneous databases

EvolutionaryTraceiP22188.
PROiP22188.

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_ECOLI
AccessioniPrimary (citable) accession number: P22188
Secondary accession number(s): O07101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.