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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen
Binding sitei29 – 291UDP-MurNAc-L-Ala-D-Glu
Binding sitei157 – 1571UDP-MurNAc-L-Ala-D-Glu
Binding sitei185 – 1851UDP-MurNAc-L-Ala-D-Glu
Binding sitei191 – 1911UDP-MurNAc-L-Ala-D-Glu
Binding sitei193 – 1931UDP-MurNAc-L-Ala-D-Glu
Binding sitei390 – 3901Meso-diaminopimelate
Binding sitei465 – 4651Meso-diaminopimelate; via carbonyl oxygen
Binding sitei469 – 4691Meso-diaminopimelate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi116 – 1227ATPSequence analysis

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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

ChEMBLiCHEMBL3309032.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 495494UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei225 – 2251N6-carboxylysine1 Publication

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 interactions.
DIPiDIP-10280N.
IntActiP22188. 20 interactions.
MINTiMINT-1230964.
STRINGi511145.b0085.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 105Combined sources
Turni11 – 133Combined sources
Beta strandi25 – 273Combined sources
Helixi29 – 313Combined sources
Beta strandi37 – 404Combined sources
Helixi48 – 514Combined sources
Helixi52 – 576Combined sources
Beta strandi61 – 666Combined sources
Turni68 – 703Combined sources
Beta strandi76 – 794Combined sources
Beta strandi82 – 876Combined sources
Helixi90 – 10112Combined sources
Helixi105 – 1073Combined sources
Beta strandi108 – 11811Combined sources
Helixi120 – 13314Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi156 – 1594Combined sources
Helixi162 – 17413Combined sources
Beta strandi179 – 1835Combined sources
Helixi186 – 1905Combined sources
Turni191 – 1966Combined sources
Beta strandi200 – 2045Combined sources
Helixi212 – 2154Combined sources
Helixi218 – 23013Combined sources
Beta strandi236 – 2405Combined sources
Helixi244 – 2507Combined sources
Beta strandi257 – 2637Combined sources
Turni267 – 2693Combined sources
Beta strandi271 – 28111Combined sources
Beta strandi286 – 2927Combined sources
Beta strandi297 – 3015Combined sources
Helixi306 – 32116Combined sources
Helixi326 – 3327Combined sources
Helixi333 – 3353Combined sources
Beta strandi342 – 3465Combined sources
Beta strandi353 – 3575Combined sources
Helixi362 – 37413Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi388 – 3903Combined sources
Helixi394 – 40512Combined sources
Beta strandi407 – 4115Combined sources
Helixi421 – 4299Combined sources
Helixi435 – 4373Combined sources
Beta strandi438 – 4403Combined sources
Helixi444 – 45411Combined sources
Beta strandi460 – 4656Combined sources
Beta strandi471 – 4744Combined sources
Beta strandi477 – 4804Combined sources
Helixi483 – 4919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E8CX-ray2.00A/B2-495[»]
ProteinModelPortaliP22188.
SMRiP22188. Positions 3-495.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22188.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 463UDP-MurNAc-L-Ala-D-Glu binding
Regioni158 – 1592UDP-MurNAc-L-Ala-D-Glu binding
Regioni414 – 4174Meso-diaminopimelate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4174Meso-diaminopimelate recognition motif

Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.Curated

Phylogenomic databases

eggNOGiENOG4107EEN. Bacteria.
COG0769. LUCA.
HOGENOMiHOG000268118.
InParanoidiP22188.
KOiK01928.
OMAiHNHNIKF.
OrthoDBiEOG6PKFCR.
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.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti344 – 3441E → K in murE1.
Natural varianti495 – 4951A → S in murE1.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1E8CX-ray2.00A/B2-495[»]
ProteinModelPortaliP22188.
SMRiP22188. Positions 3-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

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.
OrthoDBiEOG6PKFCR.
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.
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

« Hide 'large scale' publications
  1. "Nucleotide sequence of the murE gene of Escherichia coli."
    Tao J.-S., Ishiguro E.E.
    Can. J. Microbiol. 35:1051-1054(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-gamma-glutamate ligases: identification of a ligase superfamily."
    Eveland S.S., Pompliano D.L., Anderson M.S.
    Biochemistry 36:6223-6229(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT MURE1.
    Strain: CGSC 5989.
  6. "Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli."
    Michaud C., Parquet C., Flouret B., Blanot D., van Heijenoort J.
    Biochem. J. 269:277-278(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124, PROTEIN SEQUENCE OF 2-19, SEQUENCE REVISION.
  7. "Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase from Escherichia coli."
    Michaud C., Mengin-Lecreulx D., van Heijenoort J., Blanot D.
    Eur. J. Biochem. 194:853-861(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
  8. "Specificity of the uridine-diphosphate-N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate synthetase from Escherichia coli."
    Abo-Ghalia M., Michaud C., Blanot D., van Heijenoort J.
    Eur. J. Biochem. 153:81-87(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  9. "Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli."
    Mengin-Lecreulx D., Blanot D., van Heijenoort J.
    J. Bacteriol. 176:4321-4327(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: KINETIC PARAMETERS, SUBSTRATE SPECIFICITY.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli."
    Gordon E., Flouret B., Chantalat L., van Heijenoort J., Mengin-Lecreulx D., Dideberg O.
    J. Biol. Chem. 276:10999-11006(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PRODUCT, FUNCTION, CATALYTIC ACTIVITY, CARBAMOYLATION AT LYS-225.

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: July 6, 2016
This is version 157 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.