UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase - Bacillus cereus (strain ATCC 14579 / DSM 31)

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Q819Q0 (MURE_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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:	BC_3914

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [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_0000101864

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

Q819Q0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: DB23525BF0B4261E
Show »

FASTA

491

53,713

        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 FSKMVEQGVD STVMEVSSHA 

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

       250        260        270        280        290        300 
DDNVTEEYMR STAATVVTYG IDTTSDIMAK NIVMTSGGTT FTLVTPYESV NVTMKLIGKF 

       310        320        330        340        350        360 
NVYNVLAATA AGLVSGVKLE TIIAVIKDLA GVPGRFEVVD GGQNYTVIVD YAHTPDSLEN 

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

       430        440        450        460        470        480 
MVHGASGKNY EMIIDRKEAI HHAIAKAKAD DIIIIAGKGH ETYQIIGKEV HHFDDREVAK 

       490 
EAITGRLNNE E

« Hide

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.

Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP10835.1.
RefSeq	NP_833634.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q819Q0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q819Q0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000032172; EBBACP00000031378; EBBACG00000032163.
GeneID	1206259.
GenomeReviews	Gene locus BC_3914 in contig AE016877_GR.
KEGG	bce:BC3914.
PATRIC	32603865. VBIBacCer54481_4036.
Phylogenomic databases
eggNOG	COG0769.
GeneTree	EBGT00050000000629.
HOGENOM	HBG602753.
OMA	IGTIANY.
PhylomeDB	Q819Q0.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	BCER226900:BC_3914-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_BACCR

Accession

Primary (citable) accession number: Q819Q0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 68 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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents