UDP-N-acetylmuramoylalanine--D-glutamate ligase - Bacillus licheniformis (strain DSM 13 / ATCC 14580)

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Q65JY2 (MURD_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. History...

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

Documents (2) |

Third-party data

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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-acetylmuramoylalanine--D-glutamate ligase
EC=6.3.2.9

Alternative name(s):
D-glutamic acid-adding enzyme
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase

Gene names

Name:	murD
Ordered Locus Names:	BLi01737, BL02241

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) By similarity. HAMAP MF_00639
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP MF_00639
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00639
Subcellular location	Cytoplasm By similarity HAMAP MF_00639.
Sequence similarities	Belongs to the MurCDEF family.

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
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-acetylmuramoylalanine-D-glutamate 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 – 451

451

UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639

PRO_0000108965

Regions

Nucleotide binding

120 – 126

ATP Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q65JY2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: F8C603301D507BA9
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FASTA

451

49,740

        10         20         30         40         50         60 
MDTQDLLQNQ NVLVLGLAKS GYAAASILHE KGVKVVVNDQ LPFEENEPAR ILAEKGVEVV 

        70         80         90        100        110        120 
CGSHPTELFD LHSIDILIKN PGIRYENVMV EEALKRGIPV WTEVELAYHL TDAPFIGITG 

       130        140        150        160        170        180 
SNGKTTTTTL VYEMLKADSK KALVAGNIGT AASEVANQAS GDEWIVTELS SFQLMGTYQF 

       190        200        210        220        230        240 
RPKIGLLLNV FDAHLDYHHS RKNYELAKQQ VYRNQSETDV AVVNLDDETV VRLAECSKAE 

       250        260        270        280        290        300 
KVYFSVRRTL ERGACVKDGA IMFNGEPVMP LEDVVLPGEH NLENILAALC IVKTAGVSDA 

       310        320        330        340        350        360 
AVRKVLTSFT GVKHRMQYVA TIKNRLFYND SKATNILATK KALSAFQKPV ILLAGGLDRG 

       370        380        390        400        410        420 
NEFDELKPHM SFVKAVITFG ETAPKFEKLA EEMGIQQVKR VDNVEQAATA AFSLSDEGDV 

       430        440        450 
ILLSPACASW DQYKTFEERG DMFVNAVHML K

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References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A.

Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017333 Genomic DNA. Translation: AAU40632.1. CP000002 Genomic DNA. Translation: AAU23275.1.
RefSeq	YP_078913.1. NC_006270.3. YP_091325.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65JY2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65JY2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000058110; EBBACP00000056641; EBBACG00000058101. EBBACT00000061819; EBBACP00000060252; EBBACG00000061810.
GeneID	3030887. 3098426.
GenomeReviews	Gene locus BLi01737 in contig AE017333_GR. Gene locus BL02241 in contig CP000002_GR.
KEGG	bld:BLi01737. bli:BL02241.
NMPDR	fig\|279010.5.peg.1584.
PATRIC	18949073. VBIBacLic203714_1740.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0771.
GeneTree	EBGT00070000032130.
HOGENOM	HBG750024.
OMA	ACASWDM.
PhylomeDB	Q65JY2.
ProtClustDB	PRK02472.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI01737-MONOMER. BLIC279010:BL02241-MONOMER.
Family and domain databases
HAMAP	MF_00639. MurD. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR016040. NAD(P)-bd_dom. IPR005762. UDP-N-AcMur-Glu_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K01925.
PANTHER	PTHR23135:SF2. PTHR23135:SF2. 1 hit.
Pfam	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	TIGR01087. MurD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURD_BACLD

Accession

Primary (citable) accession number: Q65JY2
Secondary accession number(s): Q62VD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 59 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents