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Database: UniProt
Entry: A7ZSU9
LinkDB: A7ZSU9
Original site: A7ZSU9 
ID   RTCA_ECO24              Reviewed;         338 AA.
AC   A7ZSU9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   01-OCT-2014, entry version 49.
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=EcE24377A_3895;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-
CC       cyclic phosphodiester at the end of RNA. The mechanism of action
CC       of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by
CC       ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-
CC       N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-
CC       phosphorus in the diester linkage to produce the cyclic end
CC       product. The biological role of this enzyme is unknown but it is
CC       likely to function in some aspects of cellular RNA processing.
CC       {ECO:0000255|HAMAP-Rule:MF_00200}.
CC   -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP +
CC       diphosphate + RNA terminal-2',3'-cyclic-phosphate.
CC       {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; CP000800; ABV16896.1; -; Genomic_DNA.
DR   RefSeq; YP_001464878.1; NC_009801.1.
DR   ProteinModelPortal; A7ZSU9; -.
DR   SMR; A7ZSU9; 4-338.
DR   STRING; 331111.EcE24377A_3895; -.
DR   EnsemblBacteria; ABV16896; ABV16896; EcE24377A_3895.
DR   GeneID; 5586091; -.
DR   KEGG; ecw:EcE24377A_3895; -.
DR   PATRIC; 18297064; VBIEscCol31211_4137.
DR   eggNOG; COG0430; -.
DR   HOGENOM; HOG000015264; -.
DR   KO; K01974; -.
DR   OMA; ERTRTGH; -.
DR   OrthoDB; EOG6RNQDX; -.
DR   BioCyc; ECOL331111:GH7P-3874-MONOMER; -.
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-HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.30.360.20; -; 1.
DR   Gene3D; 3.65.10.20; -; 2.
DR   HAMAP; MF_00200; RTC; 1.
DR   InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR   InterPro; IPR023797; RNA3'_phos_cyclase_dom.
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   PANTHER; PTHR11096; PTHR11096; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 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; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    338       RNA 3'-terminal phosphate cyclase.
FT                                /FTId=PRO_1000058561.
FT   NP_BIND     283    287       ATP. {ECO:0000255|HAMAP-Rule:MF_00200}.
FT   ACT_SITE    308    308       Tele-AMP-histidine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00200}.
FT   BINDING     103    103       ATP. {ECO:0000255|HAMAP-Rule:MF_00200}.
SQ   SEQUENCE   338 AA;  35912 MW;  9250A40EC07EBEB5 CRC64;
     MKRMIALDGA QGEGGGQILR SALSLSMITG QPFTITSIRA GRAKPGLLRQ HLTAVKAAAE
     ICRATVEGAE LGSQRLVFRP GTVRGGEYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV
     SGGTDNPSAP PADFIRRVLE PLLAKIGIHQ QTTLLRHGFY PAGGGVVATE VSPVASFNTL
     QLGERGNIVQ MCGEVLLAGV PRHVAEREIA TLAGSFSLHE QNIHNLPRDQ GPGNTVSLEV
     ESENITERFF VVGEKRVSAE VVAAQLVKEV KRYLASPAAV GEYLADQLVL PMALAGAGEF
     KVAHPSCHLL TNIAVVERFL PVRFGLIETD GVTRVSIE
//
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