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

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O69290 (MURE_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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:	Cj1641

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	427 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.
Sequence caution	The sequence CAA76495.1 differs from that shown. Reason: Erroneous initiation.

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 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 – 427

427

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

PRO_0000101876

Regions

Nucleotide binding

66 – 72

ATP Potential

Region

109 – 110

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

Region

346 – 349

Meso-diaminopimelate binding By similarity

Motif

346 – 349

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

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

Binding site

136

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

Binding site

142

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

Binding site

144

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

Binding site

322

Meso-diaminopimelate By similarity

Binding site

397

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

401

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

176

N6-carboxylysine By similarity

Experimental info

Sequence conflict

1 – 3

MKL → EIK Ref.2

Sequence conflict

K → G in CAA76495. Ref.2

Sequence conflict

K → E in CAA76495. Ref.2

Sequence conflict

121

Q → L in CAA76495. Ref.2

Sequence conflict

125

Q → P in CAA76495. Ref.2

Sequence conflict

134

E → G in CAA76495. Ref.2

Sequence conflict

142

Q → P in CAA76495. Ref.2

Sequence conflict

145

I → S in CAA76495. Ref.2

Sequence conflict

166

H → R in CAA76495. Ref.2

Sequence conflict

170

E → G in CAA76495. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

O69290 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: FADBF1E67471BB24
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FASTA

427

47,721

        10         20         30         40         50         60 
MKLKLENSFI TDNTLECEKE CFFLQTTQNA KFHAQALEKG AKIIDVNECK KLLKIDEKIQ 

        70         80         90        100        110        120 
IIGITGTNGK TTTAAAIYSI LLDLGYKCGL CGTRGAFIND EQIDEKSLTT SPILKTLEYL 

       130        140        150        160        170        180 
QIATQKKCDF FIMEVSSHAL VQNRIEGLNF AAKIFTNITQ DHLDFHGTFE NYKEAKELFF 

       190        200        210        220        230        240 
TDESLKFINK DALAIKFNVR NAFTYGIENP ALYQIKAYSL EEGISTIVTN KNQTFHIDSP 

       250        260        270        280        290        300 
LLGLFNLYNL LVASACVNEL VKPDLKDLEK AISGFGGVCG RVEQVAKGVI VDFAHTPDGI 

       310        320        330        340        350        360 
EKVLDTLKNK KLIVVFGAGG DRDKTKRPLM GKIVEHFAKI AIITSDNPRS EEPKTIMEEI 

       370        380        390        400        410        420 
LSGFTKKEKV LMIEDRKEAI KKALELKEND DLVVILGKGD ETTQEIKGIK YPFSDKVVVN 


EILKNQG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.
[2]	Griffiths P.L., Connerton I.F. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-326. Strain: NCTC 11168 / Serotype O:2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35738.1. Y16882 Genomic DNA. Translation: CAA76495.1. Different initiation.
PIR	G81260.
RefSeq	YP_002345010.1. NC_002163.1.
3D structure databases
ProteinModelPortal	O69290.
ModBase	Search...
Protein-protein interaction databases
IntAct	O69290. 19 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	905914.
GenomeReviews	Gene locus Cj1641 in contig AL111168_GR.
KEGG	cje:Cj1641.
PATRIC	20060250. VBICamJej33762_1617.
Phylogenomic databases
HOGENOM	HBG602753.
OMA	GALAYVD.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1641-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_CAMJE

Accession

Primary (citable) accession number: O69290
Secondary accession number(s): Q0P7Y7, Q9PM35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 90 of the entry and version 2 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

Experimental info

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