Reviewed, UniProtKB/Swiss-Prot Q9Z8C5 (MURE_CHLPN)

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:	CPn_0418, CP_0336, CpB0434

Organism

Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]

Taxonomic identifier

83558 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydophila

Protein attributes

Sequence length	483 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: 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_0000101881
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)
	Q9Z8C5-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 3A0FEEA93EDD76ED	FASTA	483	52,720
	10 20 30 40 50 60 MDLKELLHGV QAKIYGKVRP LEVRNLTRDS RCVSVGDIFI AHKGQRYDGN DFAVDALANG 70 80 90 100 110 120 AIAIASSLYN PFLSVVQIIT PNLEELEAEL SAKYYEYPSS KLHTIGVTGT NGKTTVTCLI 130 140 150 160 170 180 KALLDSYQKP SGLLGTIEHI LGEGVIKDGF TTPTPALLQK YLATMVRQNR DAVVMEVSSI 190 200 210 220 230 240 GLASGRVAYT NFDTAVLTNI TLDHLDFHGT FETYVAAKAK LFSLVPPSGM VVINTDSPYA 250 260 270 280 290 300 SQCIESAKAP VITYGIESAA DYRATDIQLS SSGTKYTLVY GDQKIACSSS FIGKYNVYNL 310 320 330 340 350 360 LAAISTVHAS LRCDLEDLLE KIGLCQPPPG RLDPVLMGPC PVYIDYAHTP DALDNVLTGL 370 380 390 400 410 420 HELLPEGGRL IVVFGCGGDR DRSKRKLMAQ VVERYGFAVV TSDNPRSEPP EDIVNEICDG 430 440 450 460 470 480 FYSKNYFIEI DRKQAITYAL SIASDRDIVL IAGKGHEAYQ IFKHQTVAFD DKQTVCEVLA SYV

References

[1]	"Comparative genomes of Chlamydia pneumoniae and C. trachomatis." Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S. Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029.
[2]	"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39.
[3]	"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138.
[4]	"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001363 Genomic DNA. Translation: AAD18562.1. AE002161 Genomic DNA. Translation: AAF38190.1. BA000008 Genomic DNA. Translation: BAA98626.1. AE009440 Genomic DNA. Translation: AAP98365.1.
PIR	D72080. H86542.
RefSeq	NP_224618.1. NP_300475.1. NP_444885.1. NP_876708.1.
3D structure databases
SMR	Q9Z8C5. Positions 2-480.
ModBase	Search...
Genome annotation databases
GeneID	1467115. 894904. 919161. 962867.
GenomeReviews	Gene locus CPn_0418 in contig AE001363_GR. Gene locus CP_0336 in contig AE002161_GR. Gene locus CpB0434 in contig AE009440_GR. Gene locus murE in contig BA000008_GR.
KEGG	cpa:CP0336. cpn:CPn0418. cpt:CpB0434.
TIGR	CP_0336.
Phylogenomic databases
HOGENOM	HBG602753.
OMA	HTPDGIE.
PhylomeDB	Q9Z8C5.
Enzyme and pathway databases
BioCyc	CPNE115711:CP_0336-MONOMER. CPNE115713:CPN0418-MONOMER. CPNE138677:CPJ0418-MONOMER. CPNE182082:CPB0434-MONOMER.
BRENDA	6.3.2.13. 264832.
Family and domain databases
HAMAP	MF_00208. MurE. [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:3.90.190.20. Mur_ligase_C. 1 hit. 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_CHLPN

Accession

Primary (citable) accession number: Q9Z8C5
Secondary accession number(s): Q9JQA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	February 9, 2010
This is version 78 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)