Reviewed, UniProtKB/Swiss-Prot Q6G7I6 (MURA2_STAAS)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2
    EC=2.5.1.7
Alternative name(s):
    Enoylpyruvate transferase 2
    UDP-N-acetylglucosamine enolpyruvyl transferase 2
      Short name=EPT 2

Gene names

Name:	murA2
Synonyms:	murZ
Ordered Locus Names:	SAS2027

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine By similarity.
Catalytic activity	Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. HAMAP MF_00111
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00111
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the EPSP synthase family. MurA subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	UDP-N-acetylgalactosamine biosynthetic process Inferred from electronic annotation. Source: InterPro 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	UDP-N-acetylglucosamine 1-carboxyvinyltransferase 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 – 419	419	UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 HAMAP MF_00111		PRO_0000178923
Sites
	Active site	118	1	Proton donor By similarity
	Binding site	118	1	Phosphoenolpyruvate (covalent) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G7I6-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: FFB931969C3D0E4F	FASTA	419	45,105
	10 20 30 40 50 60 MAQEVIKIRG GRTLNGEVNI SGAKNSAVAI IPATLLAQGH VKLEGLPQIS DVKTLVSLLE 70 80 90 100 110 120 DLNIKASLNG MELEVDTTEI QNAALPNNKV ESLRASYYMM GAMLGRFKKC VIGLPGGCPL 130 140 150 160 170 180 GPRPIDQHIK GFKALGAEID ESSTTSMKIE AKELKGAHIF LDMVSVGATI NIMLAAVYAT 190 200 210 220 230 240 GQTVIENAAK EPEVVDVANF LTSMGANIKG AGTSTIKING VKELHGSEYQ VIPDRIEAGT 250 260 270 280 290 300 YMCIAAACGE NVILNNIVPK HVETLTAKFS ELGVNVDVRD ERIRINNNAP YQFVDIKTLV 310 320 330 340 350 360 YPGFATDLQQ PITPLLFMAN GPSFVTDTIY PERFKHVEEL KRMGANIEVD EGTATIKPST 370 380 390 400 410 LHGAEVYASD LRAGACLIIA GLIAEGVTTI YNVKHIYRGY TDIVEHLKAL GADIWTETV

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571857 Genomic DNA. Translation: CAG43835.1.
RefSeq	YP_044138.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6G7I6.
Genome annotation databases
GeneID	2862267.
GenomeReviews	Gene locus SAS2027 in contig BX571857_GR.
KEGG	sas:SAS2027.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6G7I6.
OMA	DNVIPTH.
Enzyme and pathway databases
BioCyc	SAUR282459:SAS2027-MON.
Family and domain databases
HAMAP	MF_00111. [Tree]
InterPro	IPR001986. EPSP_synthase_core. IPR005750. UDP_GlcNAc_COvinyl_MurA. [Graphical view]
Gene3D	G3DSA:3.65.10.10. EPSP_synthase. 1 hit.
PANTHER	PTHR21090:SF4. AcGlu_Tran_MurA. 1 hit.
Pfam	PF00275. EPSP_synthase. 1 hit. [Graphical view]
ProDom	PD001867. EPSP_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01072. murA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURA2_STAAS

Accession

Primary (citable) accession number: Q6G7I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 37 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)