ID   REST_BORBU              Reviewed;         449 AA.
AC   O50979;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Telomere resolvase ResT {ECO:0000303|PubMed:11804598};
DE            EC=3.1.22.- {ECO:0000269|PubMed:11804598, ECO:0000269|PubMed:12753185};
GN   Name=resT {ECO:0000303|PubMed:11804598}; OrderedLocusNames=BB_B03;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OG   Plasmid cp26 (circular 26 kb).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   FUNCTION, SUBSTRATE SPECIFICITY, NO COFACTORS, MUTAGENESIS OF TYR-335, AND
RP   DNA-BINDING.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=11804598; DOI=10.1016/s1097-2765(01)00433-6;
RA   Kobryn K., Chaconas G.;
RT   "ResT, a telomere resolvase encoded by the Lyme disease spirochete.";
RL   Mol. Cell 9:195-201(2002).
RN   [3]
RP   FUNCTION, SUBSTRATE SPECIFICITY, AND NO COFACTORS.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=12753185; DOI=10.1046/j.1365-2958.2003.03485.x;
RA   Tourand Y., Kobryn K., Chaconas G.;
RT   "Sequence-specific recognition but position-dependent cleavage of two
RT   distinct telomeres by the Borrelia burgdorferi telomere resolvase, ResT.";
RL   Mol. Microbiol. 48:901-911(2003).
CC   -!- FUNCTION: Catalyzes the conservative, sequence-specific DNA breakage
CC       and reunion reaction that generates two hairpin telomeres from a
CC       replicated telomere substrate. Breaks two phosphodiester bonds in a
CC       single DNA duplex and joins each end with the opposite DNA strand to
CC       form covalently closed hairpin telomeres (PubMed:11804598,
CC       PubMed:12753185). In vitro relaxed-circular, open-circular and
CC       linearized plasmids, but not supercoiled DNA, are all substrates
CC       (PubMed:11804598). Cleavage is position-dependent relative to conserved
CC       sequence elements (PubMed:12753185). {ECO:0000269|PubMed:11804598,
CC       ECO:0000269|PubMed:12753185}.
CC   -!- COFACTOR:
CC       Note=No cofactors were found to be necessary.
CC       {ECO:0000269|PubMed:11804598, ECO:0000269|PubMed:12753185};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000305}. Note=Found at
CC       the end of hairpin DNA molecules in the area equivalent to eukaryotic
CC       telomeres. {ECO:0000305|PubMed:11804598, ECO:0000305|PubMed:12753185}.
CC   -!- MISCELLANEOUS: This strain of B.burgdorferi has at least 12 linear
CC       replicons with covalently closed hairpin ends.
CC       {ECO:0000269|PubMed:11804598}.
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DR   EMBL; AE000792; AAC66333.1; -; Genomic_DNA.
DR   PIR; G70216; G70216.
DR   RefSeq; NP_046989.1; NC_001903.1.
DR   RefSeq; WP_010256138.1; NC_001903.1.
DR   AlphaFoldDB; O50979; -.
DR   BindingDB; O50979; -.
DR   ChEMBL; CHEMBL1667698; -.
DR   PRIDE; O50979; -.
DR   EnsemblBacteria; AAC66333; AAC66333; BB_B03.
DR   GeneID; 56568496; -.
DR   KEGG; bbu:BB_B03; -.
DR   PATRIC; fig|224326.49.peg.1592; -.
DR   HOGENOM; CLU_049289_0_0_12; -.
DR   OMA; HILMKHI; -.
DR   PRO; PR:O50979; -.
DR   Proteomes; UP000001807; Plasmid cp26.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.443.30; -; 1.
DR   InterPro; IPR038280; ResT_sf.
DR   InterPro; IPR032047; Telomere_res.
DR   Pfam; PF16684; Telomere_res; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA recombination; DNA-binding; Endonuclease; Hydrolase;
KW   Nuclease; Plasmid; Reference proteome.
FT   CHAIN           1..449
FT                   /note="Telomere resolvase ResT"
FT                   /id="PRO_0000097254"
FT   MUTAGEN         335
FT                   /note="Y->F: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11804598"
SQ   SEQUENCE   449 AA;  54295 MW;  90FB39FEAE3E4205 CRC64;
     MPPKVKIKND FEIFRKELEI LYKKYLNNEL SYLKLKEKLK ILAENHKAIL FRKDKFTNRS
     IILNLSKTRK IIKEYINLSV IERIRRDNTF LFFWKSRRIK ELKNIGIKDR KKIEELIFSN
     QMNDEKSYFQ YFIDLFVTPK WLNDYAHKYK IEKINSYRKE QIFVKINLNT YIEIIKLLLN
     QSRDIRLKFY GVLMAIGRRP VEVMKLSQFY IADKNHIRME FIAKKRENNI VNEVVFPVFA
     DPELIINSIK EIRYMEQTEN LTKEIISSNL AYSYNRLFRQ IFNNIFAPEE SVYFCRAIYC
     KFSYLAFAPK NMEMNYWITK VLGHEPNDIT TAFHYNRYVL DNLDDKADNS LLTLLNQRIY
     TYVRRKATYS TLTMDRLESL IKEHHIFDDN YIKTLIVIKN LMLKDNLETL AMVRGLNVKI
     RKAFKATYGY NYNYIKLTEY LSIIFNYKL