Q8FZP0 (MURE_BRUSU) Reviewed, UniProtKB/Swiss-Prot

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:	BR1436, BS1330_I1430

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	488 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 – 488	488	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208		PRO_0000101872
Regions
	Nucleotide binding	108 – 114	7	ATP Potential
	Region	150 – 151	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	405 – 408	4	Meso-diaminopimelate binding By similarity
	Motif	405 – 408	4	Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208
Sites
	Binding site	29	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	177	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	183	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	185	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	381	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	217	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FZP0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 420F87D1039D20A2	FASTA	488	51,376
	10 20 30 40 50 60 MKLKEIALFN ELASGEAGEV EITGITSDSR AVQRGFLFAA LKGVKADGAV FAADAVKRGA 70 80 90 100 110 120 VAIIAGKDTA IADAGVPVLH VDDPRHVLAI AAAQFYGKQP EVMVAVTGTS GKTSVASFTR 130 140 150 160 170 180 QIWAYAGFPA ANIGTTGVFS PTRSDYNSLT TPDPVELHRV LAELTSEGVT HAAMEASSHG 190 200 210 220 230 240 LDQRRLDGVR LAAGAFTNLG RDHMDYHATI DEYLGAKMRL FNALLPKGAP AIIFADDQFS 250 260 270 280 290 300 AQAIEAATLA GCDVKTVGRK GNFIALKRVE HERFRQHVEV RIGEEIFEIE LPLAGDFQVA 310 320 330 340 350 360 NALVAAGLAM VTGVPAAAAM RALALLKGAP GRLDLVGATE DGAPAYVDYA HKPEALENVL 370 380 390 400 410 420 TSVRPFTTGR VIVVFGCGGD RDKGKRPIMG EIASRLADVV IVTDDNPRSE VPAQIRSEIM 430 440 450 460 470 480 AAATGATEIG DRREAIFTAV SMMQPGDTLV VAGKGHEEGQ IVGNITLPFS DHAEVAAALA ARLEEHPK

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN30349.1. CP002997 Genomic DNA. Translation: AEM18765.1.
RefSeq	NP_698434.1. NC_004310.3. YP_005616257.1. NC_017251.1.
3D structure databases
ProteinModelPortal	Q8FZP0.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR1436.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN30349; AAN30349; BR1436. AEM18765; AEM18765; BS1330_I1430.
GeneID	1167118. 12138469.
KEGG	bms:BR1436. bsi:BS1330_I1430.
PATRIC	17791231. VBIBruSui107850_1462.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HOG000268118.
KO	K01928.
OMA	GALAYVD.
ProtClustDB	PRK00139.
Enzyme and pathway databases
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_BRUSU

Accession

Primary (citable) accession number: Q8FZP0
Secondary accession number(s): G0KBJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program