UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase - Thermosynechococcus elongatus (strain BP-1)

Contribute

Send feedback

Read comments (?) or add your own

Q8DJI4 (MURE_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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:	tlr1239

Organism

Thermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Thermosynechococcus ›

Protein attributes

Sequence length	497 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-Rule 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-Rule MF_00208
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00208
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Carbamoylation is probably crucial for Mg²⁺ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP-Rule 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 peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolylpolyglutamate biosynthetic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: HAMAP tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 497

497

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

PRO_0000101959

Regions

Nucleotide binding

113 – 119

ATP Potential

Region

155 – 156

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

Region

409 – 412

Meso-diaminopimelate binding By similarity

Motif

409 – 412

Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site

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

Binding site

182

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

Binding site

188

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

Binding site

190

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

Binding site

385

Meso-diaminopimelate By similarity

Binding site

460

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

464

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

222

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8DJI4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2F21F05584ECF07B
Show »

FASTA

497

53,933

        10         20         30         40         50         60 
MNLRELLTAA AITPGFEHPA LNQEVKSLRM NSWECEPGSL FIGMPGTRVE GGNFWPSALA 

        70         80         90        100        110        120 
AGAIAAVVSP QAKPREGEAC VIVVPDIERA CGRLAAAFYN YPSQHLSLLG VTGTNGKTTT 

       130        140        150        160        170        180 
THLVEHLLNR VGYPTALLGT LYSRWPGHCE VASHTTPFAV TLQEQLAAAV DAGCRFGVME 

       190        200        210        220        230        240 
VSSHALAQDR VWGCQFEVAA FTNLTQDHLD YHRDLEDYFA AKAKLFTADY LKGRAILNGD 

       250        260        270        280        290        300 
DPFGQRLAQQ LPRDRYWTYG LSKDADFRAE NLNYRSNGVT GAVHTPLGSG TLDSPLVGQF 

       310        320        330        340        350        360 
NVANVLAAIA MGAAVGLPLE AMLNALRDFP GVPGRMEQVR LDPEQDITVV VDYAHTPDSL 

       370        380        390        400        410        420 
ENLLRAARPF IPGKLICVFG CGGDRDRSKR PQMGAIAARL ADQVVVTSDN PRTENPQRIL 

       430        440        450        460        470        480 
DDILAGIPPE TAMIVEGDRR QAILQAILTA APGDGVIIAG KGHEDYQILG TEKVHFDDRE 

       490 
EARNALKERL KQPLQRG

« Hide

References

[1]

"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.

Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000039 Genomic DNA. Translation: BAC08791.1.
RefSeq	NP_682029.1. NC_004113.1.
3D structure databases
ProteinModelPortal	Q8DJI4.
ModBase	Search...
Protein-protein interaction databases
STRING	197221.tlr1239.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC08791; BAC08791; BAC08791.
GeneID	1011779.
KEGG	tel:tlr1239.
PATRIC	23927810. VBITheElo119873_1303.
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HOG000268118.
KO	K01928.
OMA	RPLMGEA.
ProtClustDB	PRK00139.
Enzyme and pathway databases
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.40.1190.10. 1 hit. 3.90.190.20. 1 hit.
HAMAP	MF_00208. MurE.
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
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_THEEB

Accession

Primary (citable) accession number: Q8DJI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 75 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