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

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Q253Y4 (MURE_CHLFF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. 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:	CF0632

Organism

Chlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]

Taxonomic identifier

264202 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydophila ›

Protein attributes

Sequence length	485 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
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
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 485

485

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

PRO_1000012344

Regions

Nucleotide binding

111 – 117

ATP Potential

Region

153 – 154

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-Rule MF_00208

Sites

Binding site

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

Binding site

180

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

Binding site

188

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

Binding site

382

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

220

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q253Y4 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 91A8312A531EFE64
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FASTA

485

53,404

        10         20         30         40         50         60 
MNLKELLHNI DIDAKVYGKI SPIEVRNLTK DSRNIGFGDI FIANKGKRCD GNDFASLAVE 

        70         80         90        100        110        120 
NGAIAVVSSI YNPFLSVVQI ISPNLSLLEA QLAAKYYNYP SRKLCVVGIT GTNGKTTVSH 

       130        140        150        160        170        180 
LIKFLFDACD KPSGLIGTIE HILGNNRIQD GFTTPESCLL QKYLAEMVKS NLTAAVIETS 

       190        200        210        220        230        240 
SIGLVLDRLA NVEFDVGVLT NVTLDHLDFH DSFEEYIKAK LQLFAQLSDS GLAVVNNDLP 

       250        260        270        280        290        300 
QAKQFLEATR AVPVTYGIEQ LADYRASNLR FSPFGADFDL IHKGEIFPCH SPLIGQYNVY 

       310        320        330        340        350        360 
NVLAAIAVTH QRLNCDLQQL VSLVASVKSP RGRLEPIQSG PCPIYIDYAH TPDALDNVCQ 

       370        380        390        400        410        420 
TLRTLLPSGG KLIVVFGCGG DRDRSKRKIM AQVVEKYGFA VVTSDNPRGE DPETIVNEIC 

       430        440        450        460        470        480 
SGFVKRNFSI EIDRKQAITY ALSIASDRDI VLVAGKGHET YQIFKHQTIA FDDREVVHEV 


LSSYV

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References

[1]

"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fe/C-56.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006861 Genomic DNA. Translation: BAE81404.1.
RefSeq	YP_515549.1. NC_007899.1.
3D structure databases
ProteinModelPortal	Q253Y4.
ModBase	Search...
Protein-protein interaction databases
STRING	264202.CF0632.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3958925.
KEGG	cfe:CF0632.
PATRIC	20204913. VBIChlFel51660_0661.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HOG000268118.
KO	K01928.
OMA	RPLMGEA.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	CFEL264202:GJCG-658-MONOMER.
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.40.1190.10. 1 hit. 3.90.190.20. 1 hit.
HAMAP	MF_00208. MurE.
InterPro	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_CHLFF

Accession

Primary (citable) accession number: Q253Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 18, 2006
Last modified:	May 1, 2013
This is version 57 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

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents