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O51219 (MURE_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UDP-N-acetylmuramyl-tripeptide synthetase
EC=6.3.2.-
Alternative name(s):
UDP-MurNAc-tripeptide synthetase
Gene names
Name:murE
Ordered Locus Names:BB_0201
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the addition of an amino 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

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 – 508508UDP-N-acetylmuramyl-tripeptide synthetase HAMAP MF_00208
PRO_0000101869

Regions

Nucleotide binding118 – 1247ATP Potential
Region163 – 1642UDP-MurNAc-L-Ala-D-Glu binding By similarity

Sites

Binding site351UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site2001UDP-MurNAc-L-Ala-D-Glu By similarity

Amino acid modifications

Modified residue2321N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O51219 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 44043B05F3683BBC

FASTA50857,149
        10         20         30         40         50         60 
MNKKLNEVLL KLDQDLIKCV KGSLDLEISG VTYSSKLVLP RFVFFALPGI HFDGHDFIEI 

        70         80         90        100        110        120 
AIQKGSNVVV CSRDVDFYSP NVTYIKVDDF NIRKFMSNFS NIFYDEPSKK LKVIGVTGTD 

       130        140        150        160        170        180 
GKSSVCYYIY LLFKKKGVKV GFISTVFFDD GSGSLIKNPY RQSTPESTEI HSFLSTMVKN 

       190        200        210        220        230        240 
EAQYAILEST SHGLDLETAR LIDVNYFAVV FTNIGHEHLE FHGTIQNYLN VKLGLFRSVS 

       250        260        270        280        290        300 
DDAGFGVINL DDLYSSDFKN AVKKSFTYSL KSSKADFFVS FIDEKTDSTR FEFYHKGVKY 

       310        320        330        340        350        360 
LANVSLLGSF NVENVMAALI LVSQILNIDI QDIVDKLNCI KSLDGRMDSI NLGQNFSVII 

       370        380        390        400        410        420 
DYAHTPGAFS KLFPIFKRFA TNRLISVFGS AGERDVEKRF LQGQIADIYS DLIILCDEDP 

       430        440        450        460        470        480 
RGENSMCIIK DIAKGIVNKV ENKDLFFIAD RKQAIEKAIS LAKAGDLVVA LGKGHESSII 

       490        500 
YKNREVFWNE QEVVKNAILS LEKSEKEK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66588.1.
PIRA70125.
RefSeqNP_212335.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51219.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008948; EBBORP00000008278; EBBORG00000008947.
GeneID1195036.
GenomeReviewsGene locus BB_0201 in contig AE000783_GR.
KEGGbbu:BB0201.
NMPDRfig|224326.1.peg.585.
PATRIC20557004. VBIBorBur75917_0597.
TIGRBB_0201.

Phylogenomic databases

GeneTreeEBGT00050000006937.
HOGENOMHBG602753.
OMAGADPYQK.
PhylomeDBO51219.
ProtClustDBCLSK507427.

Enzyme and pathway databases

BioCycBBUR224326:BB_0201-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_BORBU
AccessionPrimary (citable) accession number: O51219
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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