UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase - Helicobacter hepaticus (strain ATCC 51449 / 3B1)

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Q7VF14 (MURE_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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:	HH_1865

Organism

Helicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]

Taxonomic identifier

235279 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	463 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 – 463

463

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

PRO_0000101901

Regions

Nucleotide binding

94 – 100

ATP Potential

Region

137 – 138

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

Region

382 – 385

Meso-diaminopimelate binding By similarity

Motif

382 – 385

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

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

Binding site

164

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

Binding site

170

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

Binding site

172

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

Binding site

358

Meso-diaminopimelate By similarity

Binding site

433

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

437

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

204

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7VF14 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: AED726AE8A2A5AE2
Show »

FASTA

463

52,463

        10         20         30         40         50         60 
MIIKKNVSYK DRSFIALTDD TRVIESLLKG EGDKFGLQKD ADTDKVLFVK NKQNKNFITP 

        70         80         90        100        110        120 
QIAQSCSMVE SYELNDILMA NFSHNSPNIV GITGTNGKTT TAAIIYSILL DLGFNVALLG 

       130        140        150        160        170        180 
TRGFFINEHR IKPKGLTTPS MLELYENLCI AMEQKCNFFI MEVSSHAIEQ ERIAGLDFAL 

       190        200        210        220        230        240 
KILTNITSDH LDYHKSVEEY RRIKNSFFEG EGRKLLNADE PYIYCTDKAA YFYGIEKKGN 

       250        260        270        280        290        300 
LSVDVYALEN GIDGYISWRE RDYKTNEQSA IQAHLYGKHN LYNTLAAIGA VKILTQEPLE 

       310        320        330        340        350        360 
RIAEALEHFG GVSGRMEVVH NMPLVIVDFA HTYDGMYQIF ESFRHCKIAV VFGAGGDRDK 

       370        380        390        400        410        420 
SKRPKMGACA QQFAHKIYIT SDNPRTESPK SIIEDILSGM QDGEYVFVEA DRKKAIYMAL 

       430        440        450        460 
ESLESDEVLL ILGKGDEDYQ IIGNEKIYFD DREVVRNYFA SRT

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References

[1]

"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.

Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017125 Genomic DNA. Translation: AAP78462.1.
RefSeq	NP_861396.1. NC_004917.1.
3D structure databases
ProteinModelPortal	Q7VF14.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1492412.
GenomeReviews	Gene locus HH_1865 in contig AE017125_GR.
KEGG	hhe:HH1865.
NMPDR	fig\|235279.1.peg.1865.
PATRIC	20591166. VBIHelHep90276_1840.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG602753.
OMA	IGTIANY.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	HHEP235279:HH_1865-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. 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	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_HELHP

Accession

Primary (citable) accession number: Q7VF14

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 66 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