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

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Q81WC7 (MURE_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
EC=6.3.2.13

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 names

Name:	murE
Ordered Locus Names:	BA_4053, GBAA_4053, BAS3765

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP MF_00208
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208
Subcellular location	Cytoplasm By similarity HAMAP MF_00208.
Post-translational modification	Carbamoylation is probably crucial for Mg²⁺ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208
Sequence similarities	Belongs to the MurCDEF family. MurE subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 491

491

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208

PRO_0000101863

Regions

Nucleotide binding

108 – 114

ATP Potential

Region

150 – 151

UDP-MurNAc-L-Ala-D-Glu binding By similarity

Region

407 – 410

Meso-diaminopimelate binding By similarity

Motif

407 – 410

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

149

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

177

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

185

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

383

Meso-diaminopimelate By similarity

Binding site

457

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

461

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

217

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q81WC7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7E2193B06F881669
Show »

FASTA

491

53,705

        10         20         30         40         50         60 
MKLHTLVSCL HDFPVVPKEN PEITSIEADS RKVKEGSLFV CMKGYTVDSH DFAKQAAAQG 

        70         80         90        100        110        120 
AAAIVAERPI DVDVPVVLVK NTFRSLAVLA DYFYGQPTHK LHLIGITGTN GKTTTSHIMD 

       130        140        150        160        170        180 
EIMRAHGHKT GLIGTINMKI GDETFEVKNT TPDALTLQQT FAKMVEHGVD STVMEVSSHA 

       190        200        210        220        230        240 
LDLGRVHGCD YDVAVFTNLT QDHLDYHKTM EEYKHAKGLL FAQLGNSYNH NREKYAVLNN 

       250        260        270        280        290        300 
DDAVTVEYMR STAATVVTYG IDTTSDVMAK DIAMTSGGTT FTLVTPYESV NVTMKLIGKF 

       310        320        330        340        350        360 
NVYNVLAATA AGLVSGVSLE TIIDVIKELA GVPGRFEVVD GGQNYTVIVD YAHTPDSLEN 

       370        380        390        400        410        420 
VLKTAKQFAK GDVYCIVGCG GDRDRTKRPI MASVATQYAT HAIYTSDNPR SEDPAAILDD 

       430        440        450        460        470        480 
MVHGANGNNY EVIIDRKEAI HHAITKAKAD DIIIIAGKGH ETYQIIGKDV HHFDDREVAK 

       490 
EAITERLNNE E

« Hide

References

[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. Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP27779.1. AE017334 Genomic DNA. Translation: AAT33170.1. AE017225 Genomic DNA. Translation: AAT56067.1.
RefSeq	NP_846293.1. NC_003997.3. YP_020695.1. NC_007530.2. YP_030016.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81WC7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000008767; EBBACP00000008523; EBBACG00000008759. EBBACT00000016254; EBBACP00000015875; EBBACG00000016246. EBBACT00000023692; EBBACP00000023177; EBBACG00000023683.
GeneID	1086243. 2815156. 2848185.
GenomeReviews	Gene locus BA_4053 in contig AE016879_GR. Gene locus BAS3765 in contig AE017225_GR. Gene locus GBAA_4053 in contig AE017334_GR.
KEGG	ban:BA_4053. bar:GBAA_4053. bat:BAS3765.
TIGR	BA_4053. GBAA_4053.
Phylogenomic databases
GeneTree	EBGT00050000000629.
HOGENOM	HBG602753.
OMA	IGTIANY.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	BANT260799:BAS3765-MONOMER. BANT261594:GBAA4053-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K01928.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMs	TIGR01085. MurE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_BACAN

Accession

Primary (citable) accession number: Q81WC7
Secondary accession number(s): Q6HUH2, Q6KNQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents