Q6GHN7 (PYRR_STAAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein PyrR

Including the following 2 domains:

1. Pyrimidine operon regulatory protein
2. Uracil phosphoribosyltransferase
   Short name=UPRTase
   EC=2.4.2.9

Gene names

Name:	pyrR
Ordered Locus Names:	SAR1174

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	175 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes By similarity. HAMAP-Rule MF_01219 Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant By similarity. HAMAP-Rule MF_01219
Catalytic activity	UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01219
Subunit structure	Homodimer and homohexamer; in equilibrium By similarity.
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Transcription termination
Ligand	RNA-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA-dependent transcription, termination Inferred from electronic annotation. Source: HAMAP nucleoside metabolic process Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: HAMAP uracil phosphoribosyltransferase 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 – 175	175	Bifunctional protein PyrR HAMAP-Rule MF_01219		PRO_0000183056
Regions
	Region	40 – 41	2	Substrate-binding By similarity
	Region	102 – 110	9	Substrate binding By similarity
	Motif	98 – 110	13	PRPP-binding By similarity
Sites
	Binding site	135	1	Substrate By similarity
	Binding site	159	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GHN7 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 88409753D5CC5FB0	FASTA	175	19,855
	10 20 30 40 50 60 MSERIIMDDA AIQRTVTRIA HEILEYNKGT DNLILLGIKT RGEYLANRIQ DKIHQIEQQR 70 80 90 100 110 120 IPTGTIDITY FRDDIEHMSS LTTKDAIDID TDITDKVVII IDDVLYTGRT VRASLDAILL 130 140 150 160 170 NARPIKIGLA ALVDRGHREL PIRADFVGKN IPTSKEETVS VYLEEMDQRN AVIIK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MRSA252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571856 Genomic DNA. Translation: CAG40176.1.
RefSeq	YP_040585.1. NC_002952.2.
3D structure databases
ProteinModelPortal	Q6GHN7.
SMR	Q6GHN7. Positions 5-174.
ModBase	Search...
Protein-protein interaction databases
STRING	282458.SAR1174.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG40176; CAG40176; SAR1174.
GeneID	2859291.
KEGG	sar:SAR1174.
PATRIC	19545895. VBIStaAur71814_1177.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2065.
HOGENOM	HOG000245770.
KO	K02825.
OMA	RDDIKGH.
ProtClustDB	PRK05205.
Enzyme and pathway databases
BioCyc	SAUR282458:GJA5-1177-MONOMER.
Family and domain databases
HAMAP	MF_01219. PyrR.
InterPro	IPR000836. PRibTrfase_dom. IPR023050. PyrR. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
PROSITE	PS00103. PUR_PYR_PR_TRANSFER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRR_STAAR

Accession

Primary (citable) accession number: Q6GHN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program