Reviewed, UniProtKB/Swiss-Prot O84271 (MURE_CHLTR)

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):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	CT_269

Organism

Chlamydia trachomatis [Complete proteome] [HAMAP]

Taxonomic identifier

813 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Post-translational modification	Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity.
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 cell wall organization 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 483	483	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_0000101883
Regions
	Nucleotide binding	109 – 115	7	ATP Potential
	Region	151 – 152	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	403 – 406	4	Meso-diaminopimelate binding By similarity
	Motif	403 – 406	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	30	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	178	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	186	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	380	1	Meso-diaminopimelate By similarity
	Binding site	453	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	457	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	218	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O84271-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: AFD354C9E5F3FC95	FASTA	483	53,334
	10 20 30 40 50 60 MHLDQLLQNI PAKIYGKVES IPVRNLTRDS RCVGVGDIFI ARQGQFCNGN DYSSQAVANG 70 80 90 100 110 120 AIAVLSSLYN PFLSVVQIIA EDPIALEASL AARFYNNPSR HLDVIGITGT NGKTTVSCLV 130 140 150 160 170 180 RELMERSGRR TGLIGTIEHI LGENRIIDSF TTPDAILLQK YFAEMVKQNL SAAVMEVSSI 190 200 210 220 230 240 GMALGRVRET EFLAGVLTNI TSDHLDFHGS LEEYIAAKKQ FFASLPEKGI AVVNLDCEYA 250 260 270 280 290 300 PSFLNGSQAR AVSYAIHQEA DYRADRLKLY SSGSSYDIWY QGQVFPCETS LIGEHNVYNV 310 320 330 340 350 360 LASLAVVHQF LGRDFADLVR DVRFLSAPKG RLDPILLGPF PVYIDYAHTP DALDNVCRIL 370 380 390 400 410 420 LQLLPKDGRL IIVFGCGGDR DRVKRPLMAK VSEHYGFSFV TSDNPRTEDP DQIIADICKG 430 440 450 460 470 480 FSTDHYVVES DRKLAIEKAI SMASDKDIVL VAGKGHEGYQ IFKHQTIVFD DREVVCEALA ALC

References

[1]

"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001273 Genomic DNA. Translation: AAC67862.1.
PIR	B71537.
RefSeq	NP_219774.1.
3D structure databases
HSSP	HSSP built from PDB template 1E8C based on UniProtKB P22188.
ModBase	Search...
Genome annotation databases
GeneID	884854.
GenomeReviews	Gene locus CT_269 in contig AE001273_GR.
KEGG	ctr:CT269.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O84271.
OMA	FPVIVDY.
Enzyme and pathway databases
BioCyc	CTRA315277:CT269-MON.
BRENDA	6.3.2.13. 108.
Family and domain databases
HAMAP	MF_00208. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_CHLTR

Accession

Primary (citable) accession number: O84271

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)