P65456 (MURA2_STAAM) Reviewed, UniProtKB/Swiss-Prot

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:	SAV2124

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine By similarity. HAMAP MF_00111
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 HAMAP MF_00111.
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 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	UDP-N-acetylglucosamine 1-carboxyvinyltransferase 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 – 419	419	UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2 HAMAP MF_00111		PRO_0000178917
Sites
	Active site	118	1	Proton donor By similarity
Amino acid modifications
	Modified residue	118	1	2-(S-cysteinyl)pyruvic acid O-phosphothioketal By similarity

Sequences

	Sequence		Length	Mass (Da)
	P65456 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 05C1CE1332B060CC	FASTA	419	45,075
	10 20 30 40 50 60 MAQEVIKIRG GRTLNGEVNI SGAKNSAVAI IPATLLAQGH VKLEGLPQIS DVKTLVSLLE 70 80 90 100 110 120 DLNIKASLNG TELEVDTTEI 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]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu50 / ATCC 700699.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000017 Genomic DNA. Translation: BAB58286.1.
RefSeq	NP_372648.1. NC_002758.2.
3D structure databases
ProteinModelPortal	P65456.
ModBase	Search...
Protein-protein interaction databases
STRING	P65456.
2D gel databases
World-2DPAGE	0002:P65456.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000006413; EBSTAP00000006231; EBSTAG00000006412.
GeneID	1122140.
GenomeReviews	Gene locus SAV2124 in contig BA000017_GR.
KEGG	sav:SAV2124.
PATRIC	19565126. VBIStaAur52173_2198.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0766.
GeneTree	EBGT00050000024856.
HOGENOM	HBG482701.
OMA	GATIWRE.
PhylomeDB	P65456.
ProtClustDB	PRK12830.
Enzyme and pathway databases
BioCyc	SAUR158878:SAV2124-MONOMER.
Family and domain databases
HAMAP	MF_00111. MurA. [Tree]
InterPro	IPR001986. Enolpyruvate_Tfrase_dom. IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b. IPR005750. UDP_GlcNAc_COvinyl_MurA. [Graphical view]
Gene3D	G3DSA:3.65.10.10. EPSP_synthase. 2 hits.
KO	K00790.
PANTHER	PTHR21090:SF4. AcGlu_Tran_MurA. 1 hit.
Pfam	PF00275. EPSP_synthase. 1 hit. [Graphical view]
SUPFAM	SSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit.
TIGRFAMs	TIGR01072. MurA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURA2_STAAM

Accession

Primary (citable) accession number: P65456
Secondary accession number(s): Q99SD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 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