ID   ATP83_ECOLX             Reviewed;         542 AA.
AC   Q47527;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Retron Ec83 probable ATPase {ECO:0000303|PubMed:1282191};
GN   ORFNames=Ga0124318_11282;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1] {ECO:0000312|EMBL:CAA78294.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PUTATIVE FUNCTION, AND DOMAIN.
RC   STRAIN=Clinical strain 161;
RX   PubMed=1282191; DOI=10.1111/j.1365-2958.1992.tb01788.x;
RA   Lim D.;
RT   "Structure and biosynthesis of unbranched multicopy single-stranded DNA by
RT   reverse transcriptase in a clinical Escherichia coli isolate.";
RL   Mol. Microbiol. 6:3531-3542(1992).
RN   [2] {ECO:0000312|EMBL:CXYK01000012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05-2753;
RA   Hur Y.J.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION IN ANTIVIRAL DEFENSE, AND IDENTIFICATION AS A RETRON.
RC   STRAIN=05-2753;
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: Probable ATPase component of antiviral defense system retron
CC       Ec83, composed of a non-coding RNA (ncRNA), a reverse transcriptase
CC       (RT), this protein and a putative HNH endonuclease. Expression of
CC       retron Ec83 confers protection against bacteriophage T2, T4 and T6. At
CC       multiplicity of infection (MOI) of 0.02 cultures slow growth when
CC       infected with T4 but do not collapse, at MOI 2 cultures enter growth
CC       stasis. {ECO:0000269|PubMed:33157039}.
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DR   EMBL; Z12832; CAA78294.1; -; Genomic_DNA.
DR   EMBL; CXYK01000012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S28007; S28007.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13304; AAA_21; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; ATP-binding; Nucleotide-binding.
FT   CHAIN           1..542
FT                   /note="Retron Ec83 probable ATPase"
FT                   /id="PRO_0000456025"
FT   MOTIF           92..99
FT                   /note="ATP-binding"
FT                   /evidence="ECO:0000305|PubMed:1282191"
FT   CONFLICT        458..542
FT                   /note="GVRGAISSWVLENLFEVAQRPPEDKYTKLLQEYKNLVFSEKYASEDARKLGA
FT                   TLSQHFGPDDETLVELKLEIEKRIWEDDFEKDQ -> ELEEQYLLGYWRTCSKLLKGRQ
FT                   RISTQNSYRNIKI (in Ref. 1; CAA78294)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   542 AA;  61685 MW;  13EF9B0C1B1F765A CRC64;
     MEQNLPSRIT KLIKKSESGD FASSYQLYKV FGSKEYGVEP DEKMSDYFKE LSAKQLEGGQ
     LRVADIHLEN YKGFESLIMD FSMKKNSTIL VGNNGCGKST ILDAIQKGLT HLSSRLSTRS
     HNGDGIEKHE LRKGQNYASI AINYDYMGIR FPMIIATTEP GYEDRAKSNY SGINELGSIF
     KTAHSINPNV SFPLIAMYTV ERANDVSTRD IENSEEIKEA QIWDKFKAYN KSLTGKADFK
     LFFRWFKELI EIENSDNADI TALRAEIRAK EKDLDNPLLK ALLAENKNSE TTKKLLEDHQ
     NSLKVLKEKL NSYYSVNSKT LHTVEDAMYS FLPGFSNLKL QRAPLDLIVD KNNVSLSVLQ
     LSQGEKTILA LIADIARRLT LLNPNSVNPL DGTGIVLIDE IDLHLHPSWQ QNIIPRLEKT
     FKNIQFIVTT HSPQVCHTID SQNIWLLKNG QKFKAPKGVR GAISSWVLEN LFEVAQRPPE
     DKYTKLLQEY KNLVFSEKYA SEDARKLGAT LSQHFGPDDE TLVELKLEIE KRIWEDDFEK
     DQ