ID RTCA_ECOLC Reviewed; 338 AA.
AC B1IP46;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
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}; OrderedLocusNames=EcolC_0294;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000946; ACA75972.1; -; Genomic_DNA.
DR RefSeq; WP_001300557.1; NZ_MTFT01000001.1.
DR AlphaFoldDB; B1IP46; -.
DR SMR; B1IP46; -.
DR KEGG; ecl:EcolC_0294; -.
DR HOGENOM; CLU_027882_0_0_6; -.
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_1000077722"
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; 35960 MW; 1E4B20199D1389AD CRC64;
MKRMIALDGA QGEGGGQILR SALSLSMITG QPFTITGIRA GRAKPGLLRQ HLTAVKAAAE
ICRATVEGAE LGSQRLLFRP GTVRGGDYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV
SGGTDNPSAP PADFIRRVLE PLLAKMGIHQ QTTLLRHGFY PAGGGVVATE VSPVASFNTL
QLGERGNIVQ MRGEVLLAGV PRHVAEREIA TLAGSFSLHE QNIHNLPRDQ GPGNTVSLEV
ESENITERFF VVGEKRVSAE VVAAQLVKEV KRYLASTAAV GEYLADQLVL PMALAGAGEF
TVAHPSCHLL TNIAVVERFL PVRFSLIETD GVTRVSIE
//
