UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase - Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)

Contribute

Send feedback

Read comments (?) or add your own

A5I1T6 (MURE_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	CBO1457, CLC_1494

Organism

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)

Taxonomic identifier

441771 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	483 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 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.

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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 483

483

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208

PRO_1000012348

Regions

Nucleotide binding

112 – 118

ATP Potential

Region

154 – 155

UDP-MurNAc-L-Ala-D-Glu binding By similarity

Region

404 – 407

Meso-diaminopimelate binding By similarity

Motif

404 – 407

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

181

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

189

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

380

Meso-diaminopimelate By similarity

Binding site

454

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

458

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

221

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5I1T6 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 6D6B564E45A4A88C
Show »

FASTA

483

54,678

        10         20         30         40         50         60 
MNLNLILKSL EYSFIKENKK EIEKIEYDSR KVKEGDLFVC IEGYATDGHK YAKKAYDNGA 

        70         80         90        100        110        120 
KVIVCEKDLE DLSYYKDCTI IKVSDSRKAL AIMSSNYYGN PSKHIKIIGI TGTNGKTTST 

       130        140        150        160        170        180 
FMMKAILEKA GYKVGLLGTI ANYIGNKKIE SHRTTPESLE LQKLFKDMVD EKVDYCVMEV 

       190        200        210        220        230        240 
SSHSLYLDRV YGVEFKEAIF TNLTQDHLDF HKTFENYFNS KLILFKNAQN SVINIDDSYG 

       250        260        270        280        290        300 
EKVLKKALGN KITYGVEKNC DLKAENLHMH SRGVEFDTIF KNEKETIALN IPGKYNIYNA 

       310        320        330        340        350        360 
LGSIGACLLE GIPLKTIKEA LEDMPSVPGR CEIVTKNYNL GYDVIVDYAH TPDGLENILN 

       370        380        390        400        410        420 
TAREFTKGRL ISVYGCGGDR DRTKRPIMGK VGSNLSDIAI ITSDNPRTED PKLIIKDVLE 

       430        440        450        460        470        480 
GIERDNYIVV EGRRDAIRKA MEIAKENDVI VVAGKGHEDY QILKDKTIHF DEREVIEELI 


KEI

« Hide

References

[1]

"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.

Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

[2]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000727 Genomic DNA. Translation: ABS37790.1. AM412317 Genomic DNA. Translation: CAL83000.1.
RefSeq	YP_001253970.1. NC_009495.1. YP_001387358.1. NC_009698.1.
3D structure databases
ProteinModelPortal	A5I1T6.
ModBase	Search...
Protein-protein interaction databases
STRING	A5I1T6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5185712. 5400241.
GenomeReviews	Gene locus CBO1457 in contig AM412317_GR. Gene locus CLC_1494 in contig CP000727_GR.
KEGG	cbh:CLC_1494. cbo:CBO1457.
PATRIC	19364987. VBICloBot22612_1437.
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HBG602753.
OMA	IGTIANY.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	CBOT36826:CBO1457-MONOMER. CBOT441771:CLC_1494-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K01928.
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_CLOBH

Accession

Primary (citable) accession number: A5I1T6
Secondary accession number(s): A7G3J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 26, 2007
Last modified:	December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents