RTCA_ECO57
ID RTCA_ECO57 Reviewed; 342 AA.
AC P58127;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=RNA 3'-terminal phosphate cyclase;
DE Short=RNA cyclase;
DE Short=RNA-3'-phosphate cyclase;
DE EC=6.5.1.4;
GN Name=rtcA; OrderedLocusNames=Z4778, ECs4263;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; 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: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic
CC phosphodiester at the end of RNA. The mechanism of action of the enzyme
CC occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer
CC of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of
CC the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to
CC produce the cyclic end product. The biological role of this enzyme is
CC unknown but it is likely to function in some aspects of cellular RNA
CC processing (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23976, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83062,
CC ChEBI:CHEBI:83064, ChEBI:CHEBI:456215; EC=6.5.1.4;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB37686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58524.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37686.1; ALT_INIT; Genomic_DNA.
DR PIR; G91161; G91161.
DR PIR; H86007; H86007.
DR RefSeq; NP_312290.2; NC_002695.1.
DR RefSeq; WP_000827117.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58127; -.
DR SMR; P58127; -.
DR STRING; 155864.EDL933_4623; -.
DR EnsemblBacteria; AAG58524; AAG58524; Z4778.
DR EnsemblBacteria; BAB37686; BAB37686; ECs_4263.
DR GeneID; 915880; -.
DR KEGG; ece:Z4778; -.
DR KEGG; ecs:ECs_4263; -.
DR PATRIC; fig|386585.9.peg.4453; -.
DR eggNOG; COG0430; Bacteria.
DR HOGENOM; CLU_027882_0_0_6; -.
DR OMA; PKPGLSH; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 1.
DR HAMAP; MF_00200; RTC; 1.
DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR InterPro; IPR023797; RNA3'_phos_cyclase_dom.
DR InterPro; IPR037136; RNA3'_phos_cyclase_dom_sf.
DR InterPro; IPR000228; RNA3'_term_phos_cyc.
DR InterPro; IPR017770; RNA3'_term_phos_cyc_type_1.
DR InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR036553; RPTC_insert.
DR PANTHER; PTHR11096; PTHR11096; 1.
DR PANTHER; PTHR11096:SF0; PTHR11096:SF0; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 1.
DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR SUPFAM; SSF52913; SSF52913; 1.
DR SUPFAM; SSF55205; SSF55205; 2.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..342
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000156418"
FT ACT_SITE 308
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 283..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 36332 MW; 783FE7FAD7160846 CRC64;
MKRMIALDGA QGEGGGQIMR SALSLSMITG QPFTITGIRA GRAKPGLLRQ HLTAVKAATE
ICGATVEGAE LGSQRLVFRP GTVRGGDYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV
SGGTDNPSAP PADFIRRVLE PLLAKIGIHQ QTTLLRHGFY PAGGGVVATE VSPVASFNTL
QLGERGNIVQ MRGEVLLAGV PRHVAEREIA TLAASFSLHE QNIHNLPRDQ GPGNTVSLEV
ESENITERFF VVGEKRVSAE VVAAQLVKEV KRYLASPAAV GEYLADQLVL PMALAGAGQF
TVAHPSCHLL TNIAVVERFL PVRFTLAETD GVTRVMITKL TD
