ID RLUF_ECO57 Reviewed; 290 AA.
AC Q8X4L9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Dual-specificity RNA pseudouridine synthase RluF {ECO:0000250|UniProtKB:P32684};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:P32684};
DE EC=5.4.99.21 {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=23S rRNA pseudouridine(2604) synthase {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=Ribosomal large subunit pseudouridine synthase F {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=rRNA pseudouridylate synthase F {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=rRNA-uridine isomerase F {ECO:0000250|UniProtKB:P32684};
DE AltName: Full=tRNA(Tyr) pseudouridine(35) synthase {ECO:0000250|UniProtKB:P32684};
GN Name=rluF; OrderedLocusNames=Z5620, ECs5005;
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Dual specificity enzyme that catalyzes the synthesis of
CC pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35
CC in the anticodon of tRNA(Tyr). {ECO:0000250|UniProtKB:P32684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(2604) in 23S rRNA = pseudouridine(2604) in 23S rRNA;
CC Xref=Rhea:RHEA:38875, Rhea:RHEA-COMP:10093, Rhea:RHEA-COMP:10094,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.21;
CC Evidence={ECO:0000250|UniProtKB:P32684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(35) in tRNA(Tyr) = pseudouridine(35) in tRNA(Tyr);
CC Xref=Rhea:RHEA:60556, Rhea:RHEA-COMP:15607, Rhea:RHEA-COMP:15608,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:P32684};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P32684}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59221.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38428.1; -; Genomic_DNA.
DR PIR; A86095; A86095.
DR PIR; E91254; E91254.
DR RefSeq; NP_313032.1; NC_002695.1.
DR RefSeq; WP_000936361.1; NZ_VOAI01000027.1.
DR AlphaFoldDB; Q8X4L9; -.
DR SMR; Q8X4L9; -.
DR STRING; 155864.Z5620; -.
DR GeneID; 75169475; -.
DR GeneID; 914336; -.
DR KEGG; ece:Z5620; -.
DR KEGG; ecs:ECs_5005; -.
DR PATRIC; fig|386585.9.peg.5226; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_6_1_6; -.
DR OMA; YHKPKGE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02554; PseudoU_synth_RluF; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.30.70.1560; Alpha-L RNA-binding motif; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47683:SF2; S4 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01149; PSI_RSU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; RNA-binding; rRNA processing;
KW tRNA processing.
FT CHAIN 1..290
FT /note="Dual-specificity RNA pseudouridine synthase RluF"
FT /id="PRO_0000100018"
FT DOMAIN 7..72
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT REGION 105..108
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P32684"
FT REGION 187..190
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P32684"
FT REGION 241..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P32684"
SQ SEQUENCE 290 AA; 32404 MW; E5C44B68BE5C38DD CRC64;
MLPDSSVRLN KYISESGICS RREADRYIEQ GNVFLNGKRA TIGDQVKPGD VVKVNGQLIE
PREAEDLVLI ALNKPVGIVS TTEDGERDNI VDFVNHSKRV FPIGRLDKDS QGLIFLTNHG
DLVNKILRAG NDHEKEYLVT VDKPITDEFI RGMGAGVPIL GTVTKKCKVK KEAPFVFRIT
LVQGLNRQIR RMCEHFGYEV KKLERTRIMN VSLSGIPLGE WRDLTDDELI DLFKLIENSS
SEAKPKAKAK PKTAGIKRPV VKMEKTAEKG GRPASNGKRF TSPGRKKKGR
//
