Q2S530 (MURD_SALRD) Reviewed, UniProtKB/Swiss-Prot

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:	SRU_0558

Organism

Salinibacter ruber (strain DSM 13855 / M31)

Taxonomic identifier

309807 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length	460 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 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-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 – 460	460	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000257235
Regions
	Nucleotide binding	115 – 121	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2S530 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: DCC18B87498782CA	FASTA	460	49,970
	10 20 30 40 50 60 MTPDEVRRTR ATVVGGARSG RAAARLLAKV GGEVFLTEQD APSDGAAAAL DEAGVEYEFG 70 80 90 100 110 120 GHTAEALDAD VLVLSPGVPT QSNIVQQALR AGLDVYSEIE AASWFCDAPI VAITGTNGKT 130 140 150 160 170 180 TTTSLTGHVF RTAFADTLGR EAIVAGNIGY PFSDYVLETE PTDVVVLEVS SFQLDHVETF 190 200 210 220 230 240 RPRVSVLLNI TPDHLGRYDH DFEAYAQAKH NIFRNQGEGD VVVYNRDDDD VRNAAEEAAA 250 260 270 280 290 300 EQGVRPMAIT REGVPAAGAG FRDGRIVLRT DDEDDSLMPQ DELALRGRHN MYNSLAAAVS 310 320 330 340 350 360 ARVMEVENDV IRESLSGFEG VPHRLEEVHT VDDVLYVNDS KATNVNAVWY ALESFDRPIV 370 380 390 400 410 420 LIAGGRDKGN DYTDLKPLVR DQVRAVVALG ESAEKVEREL GGEAPDHSRA ETMEDALTQA 430 440 450 460 QRAAQPGDVV LLSPACSSFD MYENYEERGD TFRRLVETLL

References

[1]

"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea." Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F. Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13855 / M31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000159 Genomic DNA. Translation: ABC44279.1.
RefSeq	YP_444701.1. NC_007677.1.
3D structure databases
ProteinModelPortal	Q2S530.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2S530.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3851702.
GenomeReviews	Gene locus SRU_0558 in contig CP000159_GR.
KEGG	sru:SRU_0558.
NMPDR	fig|309807.5.peg.518.
PATRIC	23423461. VBISalRub86502_0580.
TIGR	SRU_0558.
Phylogenomic databases
eggNOG	COG0771.
HOGENOM	HBG750024.
OMA	ACASWDM.
PhylomeDB	Q2S530.
ProtClustDB	CLSK2773963.
Enzyme and pathway databases
BioCyc	SRUB309807:SRU_0558-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_SALRD

Accession

Primary (citable) accession number: Q2S530

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program