ID   RTCA_PSEAE              Reviewed;         341 AA.
AC   Q9HVJ9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=PA4585;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE004091; AAG07973.1; -; Genomic_DNA.
DR   PIR; E83072; E83072.
DR   RefSeq; NP_253275.1; NC_002516.2.
DR   RefSeq; WP_003112809.1; NZ_QZGE01000004.1.
DR   AlphaFoldDB; Q9HVJ9; -.
DR   SMR; Q9HVJ9; -.
DR   STRING; 287.DR97_1890; -.
DR   PaxDb; Q9HVJ9; -.
DR   EnsemblBacteria; AAG07973; AAG07973; PA4585.
DR   GeneID; 881010; -.
DR   KEGG; pae:PA4585; -.
DR   PATRIC; fig|208964.12.peg.4799; -.
DR   PseudoCAP; PA4585; -.
DR   HOGENOM; CLU_027882_0_0_6; -.
DR   InParanoid; Q9HVJ9; -.
DR   OMA; PKPGLSH; -.
DR   PhylomeDB; Q9HVJ9; -.
DR   BioCyc; PAER208964:G1FZ6-4679-MON; -.
DR   Proteomes; UP000002438; 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; IBA:GO_Central.
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..341
FT                   /note="RNA 3'-terminal phosphate cyclase"
FT                   /id="PRO_0000156419"
FT   ACT_SITE        308
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
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   341 AA;  36637 MW;  E7277E130981D24F CRC64;
     MRKDLIELDG SEGGGQILRS ALSLSMTSGQ PLRIRNIRGR RSRPGLLRQH LTAVRAAAEI
     CAAEVEGAEL GSRELAFRPG AIRAGDYAFA IGSAGSCSLV LQTLLPALLA ANGESRVRIS
     GGTHNPLAPP ADFLRDSWLP LLQRMGAEVD LELLRHGFVP AGGGELLARV RPARWRPLQL
     EHPGAALRRQ ARALLAGIPG HVGERELERV RQRLGWSDEE RQLEFLAEDQ GPGNALLLRI
     DCEHICATFC AFGQAGVSAE RVAEQVATQA IGWMESGCAA DEHLADQLLL PMALAGAGSF
     TTPRLSAHLQ SNRRVIERFL PVRIGDQALD GGGHRIVITS A