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Protein

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

Gene

murE

Organism
Bacillus anthracis
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

Pathway:ipeptidoglycan 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei149 – 1491UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei177 – 1771UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei185 – 1851UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei383 – 3831Meso-diaminopimelateUniRule annotation
Binding sitei457 – 4571Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
Binding sitei461 – 4611Meso-diaminopimelateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 1147ATPUniRule annotation

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

BioCyciANTHRA:MURE-MONOMER.
BANT260799:GJAJ-3823-MONOMER.
BANT261594:GJ7F-3941-MONOMER.
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:BA_4053, GBAA_4053, BAS3765
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000594 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171N6-carboxylysineUniRule annotation

Post-translational modificationi

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

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_4053.

Structurei

3D structure databases

ProteinModelPortaliQ81WC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 1512UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
Regioni407 – 4104Meso-diaminopimelate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi407 – 4104Meso-diaminopimelate recognition motif

Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiHNHNIKF.
OrthoDBiEOG6PKFCR.

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.

Q81WC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLHTLVSCL HDFPVVPKEN PEITSIEADS RKVKEGSLFV CMKGYTVDSH
60 70 80 90 100
DFAKQAAAQG AAAIVAERPI DVDVPVVLVK NTFRSLAVLA DYFYGQPTHK
110 120 130 140 150
LHLIGITGTN GKTTTSHIMD EIMRAHGHKT GLIGTINMKI GDETFEVKNT
160 170 180 190 200
TPDALTLQQT FAKMVEHGVD STVMEVSSHA LDLGRVHGCD YDVAVFTNLT
210 220 230 240 250
QDHLDYHKTM EEYKHAKGLL FAQLGNSYNH NREKYAVLNN DDAVTVEYMR
260 270 280 290 300
STAATVVTYG IDTTSDVMAK DIAMTSGGTT FTLVTPYESV NVTMKLIGKF
310 320 330 340 350
NVYNVLAATA AGLVSGVSLE TIIDVIKELA GVPGRFEVVD GGQNYTVIVD
360 370 380 390 400
YAHTPDSLEN VLKTAKQFAK GDVYCIVGCG GDRDRTKRPI MASVATQYAT
410 420 430 440 450
HAIYTSDNPR SEDPAAILDD MVHGANGNNY EVIIDRKEAI HHAITKAKAD
460 470 480 490
DIIIIAGKGH ETYQIIGKDV HHFDDREVAK EAITERLNNE E
Length:491
Mass (Da):53,705
Last modified:June 1, 2003 - v1
Checksum:i7E2193B06F881669
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP27779.1.
AE017334 Genomic DNA. Translation: AAT33170.1.
AE017225 Genomic DNA. Translation: AAT56067.1.
RefSeqiNP_846293.1. NC_003997.3.
WP_000766304.1. NZ_KN050651.1.
YP_030016.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP27779; AAP27779; BA_4053.
AAT33170; AAT33170; GBAA_4053.
AAT56067; AAT56067; BAS3765.
GeneIDi1086243.
2848185.
KEGGiban:BA_4053.
bar:GBAA_4053.
bat:BAS3765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP27779.1.
AE017334 Genomic DNA. Translation: AAT33170.1.
AE017225 Genomic DNA. Translation: AAT56067.1.
RefSeqiNP_846293.1. NC_003997.3.
WP_000766304.1. NZ_KN050651.1.
YP_030016.1. NC_005945.1.

3D structure databases

ProteinModelPortaliQ81WC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_4053.

Protocols and materials databases

DNASUi1086243.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP27779; AAP27779; BA_4053.
AAT33170; AAT33170; GBAA_4053.
AAT56067; AAT56067; BAS3765.
GeneIDi1086243.
2848185.
KEGGiban:BA_4053.
bar:GBAA_4053.
bat:BAS3765.

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiHNHNIKF.
OrthoDBiEOG6PKFCR.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciANTHRA:MURE-MONOMER.
BANT260799:GJAJ-3823-MONOMER.
BANT261594:GJ7F-3941-MONOMER.

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

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.

Entry informationi

Entry nameiMURE_BACAN
AccessioniPrimary (citable) accession number: Q81WC7
Secondary accession number(s): Q6HUH2, Q6KNQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 99 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.