ID S1QWS3_9ENTE Unreviewed; 174 AA.
AC S1QWS3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Bifunctional protein PyrR {ECO:0000256|HAMAP-Rule:MF_01219};
DE Includes:
DE RecName: Full=Pyrimidine operon regulatory protein {ECO:0000256|HAMAP-Rule:MF_01219};
DE Includes:
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219};
DE Short=UPRTase {ECO:0000256|HAMAP-Rule:MF_01219};
DE EC=2.4.2.9 {ECO:0000256|HAMAP-Rule:MF_01219};
GN Name=pyrR {ECO:0000256|HAMAP-Rule:MF_01219};
GN ORFNames=OMO_00582 {ECO:0000313|EMBL:ESK62332.1};
OS Enterococcus cecorum DSM 20682 = ATCC 43198.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK62332.1, ECO:0000313|Proteomes:UP000017415};
RN [1] {ECO:0000313|EMBL:ESK62332.1, ECO:0000313|Proteomes:UP000017415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK62332.1,
RC ECO:0000313|Proteomes:UP000017415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198)
RT (Illumina assembly).";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC activity which is not physiologically significant. {ECO:0000256|HAMAP-
CC Rule:MF_01219}.
CC -!- FUNCTION: Regulates transcriptional attenuation of the pyrimidine
CC nucleotide (pyr) operon by binding in a uridine-dependent manner to
CC specific sites on pyr mRNA. This disrupts an antiterminator hairpin in
CC the RNA and favors formation of a downstream transcription terminator,
CC leading to a reduced expression of downstream genes.
CC {ECO:0000256|HAMAP-Rule:MF_01219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01219};
CC -!- SUBUNIT: Homodimer and homohexamer; in equilibrium. {ECO:0000256|HAMAP-
CC Rule:MF_01219}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrR subfamily. {ECO:0000256|ARBA:ARBA00005565,
CC ECO:0000256|HAMAP-Rule:MF_01219}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK62332.1}.
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DR EMBL; AHYS01000003; ESK62332.1; -; Genomic_DNA.
DR RefSeq; WP_016252244.1; NZ_KI535313.1.
DR AlphaFoldDB; S1QWS3; -.
DR STRING; 44008.GCA_001318175_00959; -.
DR GeneID; 60871748; -.
DR PATRIC; fig|1121864.4.peg.2110; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_9; -.
DR OrthoDB; 9802227at2; -.
DR Proteomes; UP000017415; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01219; PyrR; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR023050; PyrR.
DR PANTHER; PTHR11608; BIFUNCTIONAL PROTEIN PYRR; 1.
DR PANTHER; PTHR11608:SF0; BIFUNCTIONAL PROTEIN PYRR; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219};
KW Reference proteome {ECO:0000313|Proteomes:UP000017415};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01219};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01219};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_01219};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW ECO:0000256|HAMAP-Rule:MF_01219};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01219}.
FT DOMAIN 5..159
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT MOTIF 96..108
FT /note="PRPP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ SEQUENCE 174 AA; 19868 MW; 8F02B0BD91BE34D9 CRC64;
MSAKEVIDSV TMKRAITRMT YEMIERNRGL EDLVLVGIKT RGIYIAQRIA QRLKQIEEIE
VPVGELDITS YRDDQKKHSS EKQESVMPVS LEGKEVILVD DVLYTGRTIR AALDAVMDYG
RPNRIGLAVL VDRGHRELPI RADYVGKNIP TSSDEEIIVE MEEIDKQDRI LINK
//
