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C5D8L9 (C5D8L9_GEOSW) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 36. Feed History...

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

Protein namesRecommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
EC=6.3.2.13 HAMAP-Rule MF_00208
Alternative name(s):
Meso-A2pm-adding enzyme HAMAP-Rule MF_00208
Meso-diaminopimelate-adding enzyme HAMAP-Rule MF_00208
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase HAMAP-Rule MF_00208
UDP-MurNAc-tripeptide synthetase HAMAP-Rule MF_00208
UDP-N-acetylmuramyl-tripeptide synthetase HAMAP-Rule MF_00208
Gene names
Name:murE HAMAP-Rule MF_00208
Ordered Locus Names:GWCH70_1016 EMBL ACS23876.1
OrganismGeobacillus sp. (strain WCH70) [Complete proteome] [HAMAP] EMBL ACS23876.1
Taxonomic identifier471223 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length490 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-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 RuleBase RU004135

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00208 RuleBase RU004135.

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. RuleBase RU003630

Belongs to the MurCDEF family. MurE subfamily. HAMAP-Rule MF_00208

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding108 – 1147ATP By similarity HAMAP-Rule MF_00208
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity HAMAP-Rule MF_00208
Region407 – 4104Meso-diaminopimelate binding By similarity HAMAP-Rule MF_00208
Motif407 – 4104Meso-diaminopimelate recognition motif By similarity HAMAP-Rule MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity HAMAP-Rule MF_00208
Binding site1491UDP-MurNAc-L-Ala-D-Glu By similarity HAMAP-Rule MF_00208
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity HAMAP-Rule MF_00208
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity HAMAP-Rule MF_00208
Binding site3831Meso-diaminopimelate By similarity HAMAP-Rule MF_00208
Binding site4571Meso-diaminopimelate; via carbonyl oxygen By similarity HAMAP-Rule MF_00208
Binding site4611Meso-diaminopimelate By similarity HAMAP-Rule MF_00208

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity HAMAP-Rule MF_00208

Sequences

Sequence LengthMass (Da)Tools
C5D8L9 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 51130A205C60C782

FASTA49054,388
        10         20         30         40         50         60 
MKLQTLLSYL HDFTTYVGEN PTITSIEMDS RQVKNGALFI CIKGFTVDGH DFAKQAVENG 

        70         80         90        100        110        120 
AVAVIAERPL DVDVPVIVVR DSRRAMAMLA DAFYGQPTHR LHLIGVTGTN GKTTTTHIIE 

       130        140        150        160        170        180 
HIARKANKKT GLIGTVHIKI GDHTYPTKNT TPESLLLQRT FKQMVDEGVD VAVMEVSSHA 

       190        200        210        220        230        240 
LHMGRVHGCD YDVAVFTNLT QDHLDYHGTM EEYRNAKGLL FAQLGNRYDH ERPKFAVLNN 

       250        260        270        280        290        300 
DDPASKYYKH MTAASVITYG IETDSDIMAK KIDIVPSGMS FDLITPNGTV RVKTRLIGLF 

       310        320        330        340        350        360 
NVYNLLAAVS ACLVSGIPLP VIVEAIEEIS GVAGRFETVD EGQNFTVIVD YAHTPDSLEN 

       370        380        390        400        410        420 
VLKTIRQFAQ KKVYVVVGCG GDRDRTKRPL MAKTAVKYAD VAIFTSDNPR SEDPEQILRD 

       430        440        450        460        470        480 
MEAGVPGERY VTIVDRKEAI YYAIEQAQEG DIILIAGKGH ETYQIIGDRV IDFDDRLVAR 

       490 
EAIKERKNIC

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References

[1]"Complete sequence of chromosome of Geopacillus sp. WCH70."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Brumm P., Mead D.A., Richardson P.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WCH70 EMBL ACS23876.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001638 Genomic DNA. Translation: ACS23876.1.
RefSeqYP_002949142.1. NC_012793.1.

3D structure databases

ProteinModelPortalC5D8L9.
ModBaseSearch...

Protein-protein interaction databases

STRING471223.GWCH70_1016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS23876; ACS23876; GWCH70_1016.
GeneID7976802.
KEGGgwc:GWCH70_1016.
PATRIC21970958. VBIGeoSp101709_1094.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycGSP471223:GH2C-1134-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
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 nameC5D8L9_GEOSW
AccessionPrimary (citable) accession number: C5D8L9
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info