Q81WC7 (MURE_BACAN) 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:	BA_4053, GBAA_4053, BAS3765

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	491 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 HAMAP-Rule MF_00208.
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 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 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 – 491	491	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208		PRO_0000101863
Regions
	Nucleotide binding	108 – 114	7	ATP Potential
	Region	150 – 151	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	407 – 410	4	Meso-diaminopimelate binding By similarity
	Motif	407 – 410	4	Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208
Sites
	Binding site	30	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	149	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	177	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	185	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	383	1	Meso-diaminopimelate By similarity
	Binding site	457	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	461	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	217	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81WC7 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 7E2193B06F881669	FASTA	491	53,705
	10 20 30 40 50 60 MKLHTLVSCL HDFPVVPKEN PEITSIEADS RKVKEGSLFV CMKGYTVDSH DFAKQAAAQG 70 80 90 100 110 120 AAAIVAERPI DVDVPVVLVK NTFRSLAVLA DYFYGQPTHK LHLIGITGTN GKTTTSHIMD 130 140 150 160 170 180 EIMRAHGHKT GLIGTINMKI GDETFEVKNT TPDALTLQQT FAKMVEHGVD STVMEVSSHA 190 200 210 220 230 240 LDLGRVHGCD YDVAVFTNLT QDHLDYHKTM EEYKHAKGLL FAQLGNSYNH NREKYAVLNN 250 260 270 280 290 300 DDAVTVEYMR STAATVVTYG IDTTSDVMAK DIAMTSGGTT FTLVTPYESV NVTMKLIGKF 310 320 330 340 350 360 NVYNVLAATA AGLVSGVSLE TIIDVIKELA GVPGRFEVVD GGQNYTVIVD YAHTPDSLEN 370 380 390 400 410 420 VLKTAKQFAK GDVYCIVGCG GDRDRTKRPI MASVATQYAT HAIYTSDNPR SEDPAAILDD 430 440 450 460 470 480 MVHGANGNNY EVIIDRKEAI HHAITKAKAD DIIIIAGKGH ETYQIIGKDV HHFDDREVAK 490 EAITERLNNE E

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP27779.1. AE017334 Genomic DNA. Translation: AAT33170.1. AE017225 Genomic DNA. Translation: AAT56067.1.
RefSeq	NP_846293.1. NC_003997.3. YP_020695.1. NC_007530.2. YP_030016.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81WC7.
ModBase	Search...
Protein-protein interaction databases
STRING	198094.BA_4053.
Protocols and materials databases
DNASU	1086243.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAP27779; AAP27779; BA_4053. AAT33170; AAT33170; GBAA_4053. AAT56067; AAT56067; BAS3765.
GeneID	1086243. 2815156. 2848185.
KEGG	ban:BA_4053. bar:GBAA_4053. bat:BAS3765.
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HOG000268118.
KO	K01928.
OMA	MAKDNGA.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	BANT260799:GJAJ-3823-MONOMER. BANT261594:GJ7F-3941-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_BACAN

Accession

Primary (citable) accession number: Q81WC7
Secondary accession number(s): Q6HUH2, Q6KNQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program