Reviewed, UniProtKB/Swiss-Prot Q6G122 (MURD_BARQU)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoylalanine--D-glutamate ligase
    EC=6.3.2.9
Alternative name(s):
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
    D-glutamic acid-adding enzyme

Gene names

Name:	murD
Ordered Locus Names:	BQ08880

Organism

Bartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]

Taxonomic identifier

803 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP UDP-N-acetylmuramoylalanine-D-glutamate ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 466	466	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000108972
Regions
	Nucleotide binding	128 – 134	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6G122-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: E02078B4F6E24915	FASTA	466	51,034
	10 20 30 40 50 60 MISCTCYKGQ KVALFGLGKS GLAAAQALMS GGAKVVAWDD NPSGVHTAKR ENIPTRDLQY 70 80 90 100 110 120 ENWSEFVALI LAPGVPLTYP QPHWVVDKAR QADIEIVGDI ELFVRARNHF LQHSGFRDQD 130 140 150 160 170 180 VPFIAITGTN GKSTTTALLA HLLEQMGYDV QMGGNIGTAI LTLKPFVKKR IYVIECSSFQ 190 200 210 220 230 240 IELTPSLQPT IGLLLNLTSD HIDRHGSFAA YVQAKRRLVT GASYAFISVD NAVCQALYQQ 250 260 270 280 290 300 LLDEGHQVGA VSKEHFVENG FYADRTKLFS VCQGQRHMLA DLADMTALRG SHNAQNALMV 310 320 330 340 350 360 LATLQALKIS DPHIEKYLAS YKGLAHRMQQ VRKMGPVLFI NDSKATNAEA SAPALSTFND 370 380 390 400 410 420 IFWIVGGQAK EGGIEALRGF FHKIRKAYLI GEAAQEFAGV IGSAFPFSMS LTLENAVHEA 430 440 450 460 TVDAMCCKAK EAVVLFSPAC ASYDQFKNYE VRGEAFVSFV MQLKES

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX897700 Genomic DNA. Translation: CAF26367.1.
RefSeq	YP_032500.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2867307.
GenomeReviews	Gene locus BQ08880 in contig BX897700_GR.
KEGG	bqu:BQ08880.
NMPDR	fig|283165.1.peg.770.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6G122.
OMA	Q6G122. SEDHLDR.
Enzyme and pathway databases
BioCyc	BQUI283165:BQ08880-MON.
BRENDA	6.3.2.9. 292235.
Family and domain databases
HAMAP	MF_00639. [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.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01087. murD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURD_BARQU

Accession

Primary (citable) accession number: Q6G122

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)