ID   RT8_ECOLX               Reviewed;         374 AA.
AC   P0DV59;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Retron Eco8 reverse transcriptase {ECO:0000303|PubMed:33157039};
DE            Short=RT {ECO:0000303|PubMed:33157039};
DE            EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000305|PubMed:33157039};
GN   Name=ret {ECO:0000305};
GN   ORFNames=ERS139198_01421 {ECO:0000303|Ref.1}, Ga0119705_103345;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1] {ECO:0000312|EMBL:CUA03353.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200499;
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA   Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA   Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA   Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA   Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA   Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA   Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN ANTIVIRAL DEFENSE, INDENTIFICATION AS A RETRON, AND MUTAGENESIS
RP   OF 200-ASP-ASP-201.
RC   STRAIN=200499;
RX   PubMed=33157039; DOI=10.1016/j.cell.2020.09.065;
RA   Millman A., Bernheim A., Stokar-Avihail A., Fedorenko T., Voichek M.,
RA   Leavitt A., Oppenheimer-Shaanan Y., Sorek R.;
RT   "Bacterial Retrons Function In Anti-Phage Defense.";
RL   Cell 183:1551-1561(2020).
CC   -!- FUNCTION: Reverse transcriptase (RT) component of antiviral defense
CC       system retron Eco8, composed of this RT, the following endonuclease and
CC       a non-coding RNA (ncRNA) encoded between them. Expression of retron
CC       Eco8 confers protection against bacteriophages T4, T6, T7 and SECphi4,
CC       SECphi6 and SECphi18. At multiplicity of infection (MOI) of 0.02
CC       cultures slow growth when infected with SECphi4 but do not collapse, at
CC       MOI 2 cultures collapse. Responsible for synthesis of msDNA (a branched
CC       molecule with RNA linked by a 2',5'-phosphodiester bond to ssDNA). The
CC       retron transcript serves as primer (from a conserved internal G
CC       residue) and template for the reaction, and codes for the RT.
CC       {ECO:0000269|PubMed:33157039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405, ECO:0000305|PubMed:33157039};
CC   -!- SIMILARITY: Belongs to the bacterial reverse transcriptase family.
CC       {ECO:0000305}.
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DR   EMBL; CYGJ01000003; CUA03353.1; -; Genomic_DNA.
DR   PROSITE; PS50878; RT_POL; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   RNA-binding; RNA-directed DNA polymerase; Transferase.
FT   CHAIN           1..374
FT                   /note="Retron Eco8 reverse transcriptase"
FT                   /id="PRO_0000456016"
FT   DOMAIN          25..252
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   MUTAGEN         200..201
FT                   /note="DD->AA: No longer protects against SECphi6
FT                   infection."
FT                   /evidence="ECO:0000269|PubMed:33157039"
SQ   SEQUENCE   374 AA;  43208 MW;  53D328070CDA073C CRC64;
     MKTKKMILVD KVFYEKILSV ESFKENIITQ SAIPKISNKE VRLISSGSKI FYAINNTSPH
     SHVQLRLNRF FLSHIPLNSA AKAFVRGGSY LKYLEPHIYG SSYCRLDISS FFNNISFDDV
     KQSLSPYIKD EYLIGTEQKL IDAILNSVGY ESPIRKDKGM IIPMGFRTSP AISNIVFRKM
     DLLIQDFCAK KGVIYSRYAD DMLFSNPRES KLLMSDYFID EISSLLSIMG FNINQSKYIS
     REKEISINGY VIENKGGNGS IGTIRLSKSK LNTVLKVTHA LAQNIPYKNI CNKYIKVRLK
     EKNIKYESKK DEFEKKYYRD QLINYLGGYR SYLISLVKFH SEYKCVNSDF IIQINGILND
     IQNHIQKIKK NRRL