ID   RT95_VIBCE              Reviewed;         315 AA.
AC   P0DV94;
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 Vc95 reverse transcriptase {ECO:0000303|PubMed:33157039};
DE            Short=RT-Vc95 {ECO:0000303|PubMed:10564503};
DE            EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
GN   Name=ret {ECO:0000305};
GN   ORFNames=Ga0059260_01849, KV36_09050 {ECO:0000303|Ref.1};
OS   Vibrio cholerae serotype O1 biovar El Tor.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=686;
RN   [1] {ECO:0000312|EMBL:KFZ34334.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAK676;
RA   Kritzky A., Cheldyshova N.B., Kulshan T.A., Krasnov Y.M., Cherkasov A.V.,
RA   Smirnova N.I.;
RT   "Vibrio cholerae O1 biovar El Tor MAK676 whole genome shotgun sequence.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION, AND PROBABLE FUNCTION.
RC   STRAIN=O139;
RX   PubMed=10564503; DOI=10.1046/j.1365-2958.1999.01531.x;
RA   Shimamoto T., Kobayashi M., Tsuchiya T., Shinoda S., Kawakami H.,
RA   Inouye S., Inouye M.;
RT   "A retroelement in Vibrio cholerae.";
RL   Mol. Microbiol. 34:631-632(1999).
RN   [3]
RP   FUNCTION IN ANTIVIRAL DEFENSE, AND INDENTIFICATION AS A RETRON.
RC   STRAIN=MAK676;
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 Vc95, composed of a non-coding RNA (ncRNA), this reverse
CC       transcriptase (RT), a probable ATPase and a putative HNH endonuclease.
CC       Expression of retron Vc95 confers protection against bacteriophages T2,
CC       T4 and T6. At multiplicity of infection (MOI) of 0.02 cultures slow
CC       growth when infected with T4 but do not collapse, at MOI 2 cultures
CC       enter growth stasis (PubMed:33157039). Responsible for synthesis of
CC       msDNA (a branched molecule with RNA linked by a 2',5'-phosphodiester
CC       bond to ssDNA). The retron transcript serves as primer (from a
CC       conserved internal G residue) and template for the reaction, and codes
CC       for the RT (By similarity). The DNA segment is predicted to be 95 bases
CC       long (Probable). {ECO:0000250|UniProtKB:P21325,
CC       ECO:0000269|PubMed:33157039, ECO:0000305|PubMed:10564503}.
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; JRBD01000006; KFZ34334.1; -; Genomic_DNA.
PE   1: Evidence at protein level;
KW   Antiviral defense; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   RNA-binding; RNA-directed DNA polymerase; Transferase.
FT   CHAIN           1..315
FT                   /note="Retron Vc95 reverse transcriptase"
FT                   /id="PRO_0000456022"
FT   DOMAIN          19..244
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ   SEQUENCE   315 AA;  36388 MW;  5711FE97ECC90425 CRC64;
     MNILTTLREQ LLTNNVIMPQ EFERLEVRGS HAYKVYSIPK RKAGRRTIAH PSSKLKICQR
     HLNAILNPLL KVHDSSYAYV KGRSIKDNAL VHSHSAYVLK MDFQNFFNSI TPTILRQCLI
     QNDILLSVNE LEKLEQLIFW NPSKKRNGKL ILSVGSPISP LISNAIMYPF DKIINDICTK
     HGINYTRYAD DITFSTNIKN TLNKLPEIVE QLIIQTYAGR IIINKRKTVF SSKKHNRHVT
     GITLTNDSKI SIGRSRKRYI SSLVFKYINK NLDIDEINHM KGMLAFAYNI EPIYIHRLSH
     KYKVNIVEKI LRGSN