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Q03523 (MURE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:BSU15180
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceInferred 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101866

Regions

Nucleotide binding109 – 1157ATP Potential
Region151 – 1522UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region408 – 4114Meso-diaminopimelate binding By similarity
Motif408 – 4114Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site311UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1501UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1781UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3841Meso-diaminopimelate By similarity
Binding site4581Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4621Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03523 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: AD5458EB6DF1C1B0

FASTA49454,326
        10         20         30         40         50         60 
MKLTKLLTYL TTEPSVNDSQ DPEITSIEMD SREVKKGSLF VCVKGYTVDG HDFAQKAVEN 

        70         80         90        100        110        120 
GAAAIVAERE VDVNVPVIIV RQSLRALSVL SDAFYGQPTK KLQLIGITGT NGKTSTTHMV 

       130        140        150        160        170        180 
DEILKKAGKR TGLIGTMYMK IGDETLPVKN TTPESVTLQK TFKKMNDKHV DTAIMEVSSH 

       190        200        210        220        230        240 
ALSLGRVHGC DYDIAVFTNL TQDHLDYHKT MDEYRHAKSL LFSQLGGAFN HEHPKRAVLN 

       250        260        270        280        290        300 
ADDEASAYFE KVTAAHISTY GIKNDADVMA KNISITAQGT SFDLVTNKGT KHITMSLVGQ 

       310        320        330        340        350        360 
FNVYNVLAAV ATCIAAGIPF EIITEAVEEL HGVRGRFELV NQQQEFPVIV DYAHTPDSLE 

       370        380        390        400        410        420 
NVLETCRDMT EGKLFVVVGC GGDRDKTKRP KMAKIAVELA DEPIFTSDNP RSEDPRAILR 

       430        440        450        460        470        480 
DMEAGVENAY YHSIANREQA IFFAIANAKK GDVVLIAGKG HETYQQIGNE TFDFDDAEVA 

       490 
ARAIVELNKN KTNS

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of the murE-murD region of Bacillus subtilis 168."
Daniel R.A., Errington J.
J. Gen. Microbiol. 139:361-370(1993) [PubMed: 8436954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis."
Daniel R.A., Drake S., Buchanan C.E., Scholle R., Errington J.
J. Mol. Biol. 235:209-220(1994) [PubMed: 8289242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z15056 Genomic DNA. Translation: CAA78767.1.
AL009126 Genomic DNA. Translation: CAB13391.1.
Z25865 Genomic DNA. Translation: CAA81086.1.
PIRB47691.
RefSeqNP_389401.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ03523.
SMRQ03523. Positions 1-489.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002053; EBBACP00000002053; EBBACG00000002050.
GeneID937567.
GenomeReviewsGene locus BSU15180 in contig AL009126_GR.
KEGGbsu:BSU15180.
NMPDRfig|224308.1.peg.1520.
PATRIC18974841. VBIBacSub10457_1612.

Organism-specific databases

GenoListBSU15180. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000629.
HOGENOMHBG602753.
OMASCANAAG.
PhylomeDBQ03523.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycBSUB:BSU15180-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KOK01928.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. MurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_BACSU
AccessionPrimary (citable) accession number: Q03523
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents