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Protein

UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase

Gene

mpl

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

Functioni

Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro.2 Publications

Catalytic activityi

ATP + UDP-N-acetyl-alpha-D-muramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 Publication

Kineticsi

kcat is 290 min(-1).1 Publication

  1. KM=0.25 mM for UDP-N-acetyl-alpha-D-muramate1 Publication
  2. KM=0.19 mM for ATP1 Publication
  3. KM=0.1 mM for L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate1 Publication
  1. Vmax=5.8 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.4.1 Publication

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi110 – 1167ATPUniRule annotation

GO - Molecular functioni

  • acid-amino acid ligase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-HAMAP
  • identical protein binding Source: IntAct

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

BioCyciEcoCyc:EG12440-MONOMER.
ECOL316407:JW4192-MONOMER.
MetaCyc:EG12440-MONOMER.
BRENDAi6.3.2.B21. 2026.
UniPathwayiUPA00544.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligaseUniRule annotation (EC:6.3.2.45UniRule annotation1 Publication)
Alternative name(s):
Murein peptide ligaseUniRule annotation
UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligaseUniRule annotation
Gene namesi
Name:mpl1 PublicationUniRule annotation
Synonyms:yjfG
Ordered Locus Names:b4233, JW4192
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12440. mpl.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Enzyme ligase activity totally absent. No effect on growth.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligasePRO_0000101708Add
BLAST

Proteomic databases

EPDiP37773.
PaxDbiP37773.
PRIDEiP37773.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-562735,EBI-562735

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259323. 187 interactions.
DIPiDIP-10246N.
IntActiP37773. 7 interactions.
STRINGi511145.b4233.

Structurei

3D structure databases

ProteinModelPortaliP37773.
SMRiP37773. Positions 1-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MurCDEF family. Mpl subfamily.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105DFU. Bacteria.
COG0773. LUCA.
HOGENOMiHOG000256032.
InParanoidiP37773.
KOiK02558.
OMAiCDANVYP.
OrthoDBiEOG64BQ73.
PhylomeDBiP37773.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.40.50.720. 1 hit.
3.90.190.20. 1 hit.
HAMAPiMF_02020. Mpl.
InterProiIPR005757. Mpl.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR016040. NAD(P)-bd_dom.
[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.
TIGRFAMsiTIGR01081. mpl. 1 hit.

Sequencei

Sequence statusi: Complete.

P37773-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIHILGICG TFMGGLAMLA RQLGHEVTGS DANVYPPMST LLEKQGIELI
60 70 80 90 100
QGYDASQLEP QPDLVIIGNA MTRGNPCVEA VLEKNIPYMS GPQWLHDFVL
110 120 130 140 150
RDRWVLAVAG THGKTTTAGM ATWILEQCGY KPGFVIGGVP GNFEVSAHLG
160 170 180 190 200
ESDFFVIEAD EYDCAFFDKR SKFVHYCPRT LILNNLEFDH ADIFDDLKAI
210 220 230 240 250
QKQFHHLVRI VPGQGRIIWP ENDINLKQTM AMGCWSEQEL VGEQGHWQAK
260 270 280 290 300
KLTTDASEWE VLLDGEKVGE VKWSLVGEHN MHNGLMAIAA ARHVGVAPAD
310 320 330 340 350
AANALGSFIN ARRRLELRGE ANGVTVYDDF AHHPTAILAT LAALRGKVGG
360 370 380 390 400
TARIIAVLEP RSNTMKMGIC KDDLAPSLGR ADEVFLLQPA HIPWQVAEVA
410 420 430 440 450
EACVQPAHWS GDVDTLADMV VKTAQPGDHI LVMSNGGFGG IHQKLLDGLA

KKAEAAQ
Length:457
Mass (Da):49,874
Last modified:July 15, 1998 - v3
Checksum:i105383EA5B696844
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97130.1.
U00096 Genomic DNA. Translation: AAC77190.1.
AP009048 Genomic DNA. Translation: BAE78233.1.
X12545 mRNA. No translation available.
PIRiS56459.
RefSeqiNP_418654.1. NC_000913.3.
WP_001219813.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77190; AAC77190; b4233.
BAE78233; BAE78233; BAE78233.
GeneIDi948752.
KEGGiecj:JW4192.
eco:b4233.
PATRICi32124039. VBIEscCol129921_4364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97130.1.
U00096 Genomic DNA. Translation: AAC77190.1.
AP009048 Genomic DNA. Translation: BAE78233.1.
X12545 mRNA. No translation available.
PIRiS56459.
RefSeqiNP_418654.1. NC_000913.3.
WP_001219813.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37773.
SMRiP37773. Positions 1-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259323. 187 interactions.
DIPiDIP-10246N.
IntActiP37773. 7 interactions.
STRINGi511145.b4233.

Proteomic databases

EPDiP37773.
PaxDbiP37773.
PRIDEiP37773.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77190; AAC77190; b4233.
BAE78233; BAE78233; BAE78233.
GeneIDi948752.
KEGGiecj:JW4192.
eco:b4233.
PATRICi32124039. VBIEscCol129921_4364.

Organism-specific databases

EchoBASEiEB2335.
EcoGeneiEG12440. mpl.

Phylogenomic databases

eggNOGiENOG4105DFU. Bacteria.
COG0773. LUCA.
HOGENOMiHOG000256032.
InParanoidiP37773.
KOiK02558.
OMAiCDANVYP.
OrthoDBiEOG64BQ73.
PhylomeDBiP37773.

Enzyme and pathway databases

UniPathwayiUPA00544.
BioCyciEcoCyc:EG12440-MONOMER.
ECOL316407:JW4192-MONOMER.
MetaCyc:EG12440-MONOMER.
BRENDAi6.3.2.B21. 2026.

Miscellaneous databases

PROiP37773.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.40.50.720. 1 hit.
3.90.190.20. 1 hit.
HAMAPiMF_02020. Mpl.
InterProiIPR005757. Mpl.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR016040. NAD(P)-bd_dom.
[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.
TIGRFAMsiTIGR01081. mpl. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene."
    Hamilton W.D.O., Harrison D.A., Dyer T.A.
    Nucleic Acids Res. 16:8707-8707(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
  5. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan."
    Mengin-Lecreulx D., van Heijenoort J., Park J.T.
    J. Bacteriol. 178:5347-5352(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, CHARACTERIZATION.
    Strain: K12 / K10.
  7. "Biochemical characterization and physiological properties of Escherichia coli UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase."
    Herve M., Boniface A., Gobec S., Blanot D., Mengin-Lecreulx D.
    J. Bacteriol. 189:3987-3995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiMPL_ECOLI
AccessioniPrimary (citable) accession number: P37773
Secondary accession number(s): P76804, Q2M673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1998
Last modified: April 13, 2016
This is version 138 of the entry and version 3 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.