UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase - Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)

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Q9K9S4 (MURE_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. 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:	BH2571

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	486 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
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 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 – 486

486

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

PRO_0000101865

Regions

Nucleotide binding

109 – 115

ATP Potential

Region

151 – 152

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

Region

405 – 408

Meso-diaminopimelate binding By similarity

Motif

405 – 408

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

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

Binding site

150

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

Binding site

178

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

Binding site

186

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

Binding site

381

Meso-diaminopimelate By similarity

Binding site

455

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

459

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

218

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9K9S4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A1062ED0C3A2D2CF
Show »

FASTA

486

53,658

        10         20         30         40         50         60 
MVKLVSLLDS LYGYKMIHEG NPDIHSIHMD SREVVEGGLF FCIKGYTVDG HDYAQQAVSN 

        70         80         90        100        110        120 
GAVAVVSERP LELSVPVVVV RDSRRAMAQV ATKFYGEPTN DLQLIGVTGT NGKTTITHLI 

       130        140        150        160        170        180 
EKIMQDQGKM TGLIGTMYTK IGHELKETKN TTPESLVLQR TFADMKKSGV TTAMMEVSSH 

       190        200        210        220        230        240 
ALQSGRVRGC DFDVAVFSNL TPDHLDYHGT MERYKFAKGL LFAQLGNTYQ GKVAVLNADD 

       250        260        270        280        290        300 
PASADFAEMT IAQVVTYGIE NEADFQAENV RITSTGTTFE LAAFEERMEL SIHLIGKFSV 

       310        320        330        340        350        360 
YNVLAAAAAA YVSGVPLQEI KKSLEEVKGV AGRFETVKHD QPFTVIVDYA HTPDSLENVL 

       370        380        390        400        410        420 
KTVGELAKGD VRVVVGCGGD RDKTKRPVMA EIATTFANQA IFTSDNPRSE EPMDILRDME 

       430        440        450        460        470        480 
QGAKGDSYLM IEDRKEAIFK AIELAKEDDI IVIAGKGHET YQQFRDRTID FDDRIVAQQA 


IKERWT

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References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB06290.1.
PIR	C83971.
RefSeq	NP_243437.1. NC_002570.2.
3D structure databases
ProteinModelPortal	Q9K9S4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000053889; EBBACP00000052528; EBBACG00000053880.
GeneID	893169.
GenomeReviews	Gene locus BH2571 in contig BA000004_GR.
KEGG	bha:BH2571.
NMPDR	fig\|272558.1.peg.2571.
PATRIC	18942338. VBIBacHal18977_2682.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000000629.
HOGENOM	HBG602753.
OMA	TNLARDH.
PhylomeDB	Q9K9S4.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	BHAL272558:BH2571-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
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]
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_BACHD

Accession

Primary (citable) accession number: Q9K9S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 78 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

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents