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