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RT72_SALH5
ID   RT72_SALH5              Reviewed;         379 AA.
AC   P0DV89;
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 Se72 reverse transcriptase {ECO:0000303|PubMed:33157039};
DE            Short=RT {ECO:0000303|PubMed:33157039};
DE            EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
GN   Name=ret {ECO:0000305};
GN   ORFNames=Ga0072986_12846, SEEH8310_20099 {ECO:0000303|Ref.1};
OS   Salmonella heidelberg (strain 579083-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1054962;
RN   [1] {ECO:0000312|EMBL:KJT75256.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=579083-10;
RA   Timme R.E., Allard M., Luo Y., Strain E., Pettengill J., Li C., Ottesen A.,
RA   Brown E.;
RT   "Serovar diversity of Salmonella subsp. enterica.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN ANTIVIRAL DEFENSE, AND INDENTIFICATION AS A RETRON.
RC   STRAIN=579083-10;
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 Se72, composed of a non-coding RNA (ncRNA), this reverse
CC       transcriptase (RT) and the following cold shock-like protein.
CC       Expression of retron Se72 confers protection against bacteriophage
CC       lambda. At multiplicity of infection (MOI) of 0.02 cultures slow growth
CC       when infected with lambda but do not collapse, at MOI 2 cultures enter
CC       growth stasis (PubMed:33157039). Responsible for synthesis of msDNA (a
CC       branched molecule with RNA linked by a 2',5'-phosphodiester bond to
CC       ssDNA). The retron transcript serves as primer (from a conserved
CC       internal G residue) and template for the reaction, and codes for the RT
CC       (By similarity). The DNA segment is predicted to be 72 bases long
CC       (Probable). {ECO:0000250|UniProtKB:P21325, ECO:0000269|PubMed:33157039,
CC       ECO:0000305|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};
CC   -!- SIMILARITY: Belongs to the bacterial reverse transcriptase family.
CC       {ECO:0000305}.
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DR   EMBL; AMMS01000284; KJT75256.1; -; 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..379
FT                   /note="Retron Se72 reverse transcriptase"
FT                   /id="PRO_0000456021"
FT   DOMAIN          1..245
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ   SEQUENCE   379 AA;  43958 MW;  4A33CD21F35F9CDE CRC64;
     MNKPRFNGTP VASLDSLSAM LGIERKRLDW IVKSVSMSYK QFKVETGKNK KERQIFEPKR
     SLKGIQKKIN KEIFEKIDYP HYLHGALSGR DYISNAAVHT RKRTVICLDI TNFYPSISKK
     DVCSIFKNLM RFSPDVSLCL TELVTLNNKV PQGGCCSSYI ANLLFFNSEY NLYNRLKSMG
     LSYSRLLDDI TISSDKDLSS EEKTKVIKLV HGMVNQYRLS INESKTTIEH SKDSSSKLSV
     TGLWVKHGVP KLTKENRRYI RYLVYICKKQ GAYERHTKEY HDLWNRCSGK VAQMSRLGHV
     QAVELRAILS EIMPVYDDYK ISKLKLMAKH YLNKFTPPLT DDQIRKIDRM LYDFDIVGRT
     NKNLAKLYRR KLVALLPDR
 
 
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