ID RTCA_ECOL5 Reviewed; 338 AA. AC Q0TC48; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=RNA 3'-terminal phosphate cyclase {ECO:0000255|HAMAP-Rule:MF_00200}; DE Short=RNA cyclase {ECO:0000255|HAMAP-Rule:MF_00200}; DE Short=RNA-3'-phosphate cyclase {ECO:0000255|HAMAP-Rule:MF_00200}; DE EC=6.5.1.4 {ECO:0000255|HAMAP-Rule:MF_00200}; GN Name=rtcA {ECO:0000255|HAMAP-Rule:MF_00200}; GN OrderedLocusNames=ECP_3505; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=536 / UPEC; RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). 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. {ECO:0000255|HAMAP-Rule:MF_00200}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00200}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00200}. CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00200}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000247; ABG71481.1; -; Genomic_DNA. DR RefSeq; WP_011579219.1; NC_008253.1. DR AlphaFoldDB; Q0TC48; -. DR SMR; Q0TC48; -. DR KEGG; ecp:ECP_3505; -. DR HOGENOM; CLU_027882_0_0_6; -. DR Proteomes; UP000009182; 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; 3.65.10.20; RNA 3'-terminal phosphate cyclase domain; 1. DR Gene3D; 3.30.360.20; RNA 3'-terminal phosphate cyclase, insert domain; 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 NCBIfam; TIGR03399; RNA_3prim_cycl; 1. DR PANTHER; PTHR11096; RNA 3' TERMINAL PHOSPHATE CYCLASE; 1. DR PANTHER; PTHR11096:SF0; RNA 3'-TERMINAL PHOSPHATE CYCLASE; 1. DR Pfam; PF01137; RTC; 1. DR Pfam; PF05189; RTC_insert; 1. DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 2. DR SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 1. DR PROSITE; PS01287; RTC; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding. FT CHAIN 1..338 FT /note="RNA 3'-terminal phosphate cyclase" FT /id="PRO_0000264795" FT ACT_SITE 308 FT /note="Tele-AMP-histidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200" FT BINDING 103 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200" FT BINDING 283..287 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200" SQ SEQUENCE 338 AA; 35826 MW; B9E51039B6B7F27B CRC64; MKRMIALDGA QGEGGGQILR SALSLSMITG QPFTITGIRA GRAKPGLLRQ HLTAVKAAAE ICRATVEGAE LGSQRLVFRP GTVRGGDYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV SGGTDNPSAP PADFIRRVLE PLLAKIGVHQ QTTLLRHGFY PAGGGVVATE VSPVASFNSL QLGERGNIVQ MRGEVLLAGV PRHVAEREIA TLAASFSLHE QAVHSLPRDQ GPGNTVSLEV ESENITERFF VVGEKRVSAE VVAAQLVKEV KRYLASPAAV GEYLADQLVL PMALAGTGEF TVAHPSCHLL TNIAVVERFL PVRFGLIETD GVTRVSIE //