ID   TNR1_ECOLI              Reviewed;         183 AA.
AC   P03012;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   28-JUN-2023, entry version 154.
DE   RecName: Full=Transposon gamma-delta resolvase;
DE   AltName: Full=Transposon Tn1000 resolvase;
GN   Name=tnpR; OrderedLocusNames=ECOK12F009;
OS   Escherichia coli (strain K12).
OG   Plasmid F.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6292730; DOI=10.1038/300381a0;
RA   Reed R.R., Shibuya G.I., Steitz J.A.;
RT   "Nucleotide sequence of gamma delta resolvase gene and demonstration that
RT   its gene product acts as a repressor of transcription.";
RL   Nature 300:381-383(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8080658; DOI=10.1266/jjg.69.269;
RA   Maekawa T., Ohtsubo E.;
RT   "Identification of the region that determines the specificity of binding of
RT   the transposases encoded by Tn3 and gamma delta to the terminal inverted
RT   repeat sequences.";
RL   Jpn. J. Genet. 69:269-285(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7612932; DOI=10.3109/10425179509029361;
RA   Broom J.E., Hill D.F., Hughes G., Jones W.A., McNaughton J.C.,
RA   Stockwell P.A., Petersen G.B.;
RT   "Sequence of a transposon identified as Tn1000 (gamma delta).";
RL   DNA Seq. 5:185-189(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / CR63; PLASMID=F;
RA   Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT   "Complete nucleotide sequence of the F plasmid: its implications for
RT   organization and diversification of plasmid genomes.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   ACTIVE SITE SER-10.
RX   PubMed=6099239; DOI=10.1101/sqb.1984.049.01.028;
RA   Reed R.R., Moser C.D.;
RT   "Resolvase-mediated recombination intermediates contain a serine residue
RT   covalently linked to DNA.";
RL   Cold Spring Harb. Symp. Quant. Biol. 49:245-249(1984).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=6088082; DOI=10.1016/0092-8674(84)90501-4;
RA   Newman B.J., Grindley N.D.F.;
RT   "Mutants of the gamma delta resolvase: a genetic analysis of the
RT   recombination function.";
RL   Cell 38:463-469(1984).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-140.
RX   PubMed=2175678; DOI=10.1016/0092-8674(90)90427-g;
RA   Sanderson M.R., Freemont P.S., Rice P.A., Goldman A., Hatfull G.F.,
RA   Grindley N.D.F., Steitz T.A.;
RT   "The crystal structure of the catalytic domain of the site-specific
RT   recombination enzyme gamma delta resolvase at 2.7-A resolution.";
RL   Cell 63:1323-1329(1990).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=7628011; DOI=10.1016/0092-8674(95)90307-0;
RA   Yang W., Steitz T.A.;
RT   "Crystal structure of the site-specific recombinase gamma delta resolvase
RT   complexed with a 34 bp cleavage site.";
RL   Cell 82:193-207(1995).
RN   [9]
RP   STRUCTURE BY NMR OF 141-183.
RX   PubMed=7987224; DOI=10.1002/pro.5560030815;
RA   Liu T., Derose E.F., Mullen G.P.;
RT   "Determination of the structure of the DNA binding domain of gamma delta
RT   resolvase in solution.";
RL   Protein Sci. 3:1286-1295(1994).
CC   -!- FUNCTION: This protein catalyzes the site-specific recombination of the
CC       transposon and also regulates its frequency of transposition.
CC   -!- SIMILARITY: Belongs to the site-specific recombinase resolvase family.
CC       {ECO:0000305}.
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DR   EMBL; J01844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X60200; CAA42759.1; -; Genomic_DNA.
DR   EMBL; D16449; BAA03915.1; -; Genomic_DNA.
DR   EMBL; AP001918; BAA97879.1; -; Genomic_DNA.
DR   PIR; A03542; RPECTG.
DR   RefSeq; NP_061388.1; NC_002483.1.
DR   RefSeq; WP_001235704.1; NZ_JACEFS010000062.1.
DR   PDB; 1GDR; X-ray; 3.50 A; A=1-140.
DR   PDB; 1GDT; X-ray; 3.00 A; A/B=1-183.
DR   PDB; 1GHT; NMR; -; A=1-105.
DR   PDB; 1HX7; NMR; -; A=1-105.
DR   PDB; 1RES; NMR; -; A=141-183.
DR   PDB; 1RET; NMR; -; A=141-183.
DR   PDB; 1ZR2; X-ray; 3.90 A; A/B=1-183.
DR   PDB; 1ZR4; X-ray; 3.40 A; A/B/D/E=1-183.
DR   PDB; 2GM4; X-ray; 3.50 A; A/B=1-183.
DR   PDB; 2GM5; X-ray; 2.10 A; A/B/C/D=2-134.
DR   PDB; 2RSL; X-ray; 2.30 A; A/B/C=1-140.
DR   PDBsum; 1GDR; -.
DR   PDBsum; 1GDT; -.
DR   PDBsum; 1GHT; -.
DR   PDBsum; 1HX7; -.
DR   PDBsum; 1RES; -.
DR   PDBsum; 1RET; -.
DR   PDBsum; 1ZR2; -.
DR   PDBsum; 1ZR4; -.
DR   PDBsum; 2GM4; -.
DR   PDBsum; 2GM5; -.
DR   PDBsum; 2RSL; -.
DR   AlphaFoldDB; P03012; -.
DR   BMRB; P03012; -.
DR   SMR; P03012; -.
DR   DIP; DIP-61217N; -.
DR   PATRIC; fig|83333.107.peg.594; -.
DR   OrthoDB; 9797501at2; -.
DR   PhylomeDB; P03012; -.
DR   EvolutionaryTrace; P03012; -.
DR   PRO; PR:P03012; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   CDD; cd03768; SR_ResInv; 1.
DR   Gene3D; 6.10.250.10; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.1390; Resolvase, N-terminal catalytic domain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR006118; Recombinase_CS.
DR   InterPro; IPR006119; Resolv_N.
DR   InterPro; IPR036162; Resolvase-like_N_sf.
DR   InterPro; IPR006120; Resolvase_HTH_dom.
DR   PANTHER; PTHR30461; DNA-INVERTASE FROM LAMBDOID PROPHAGE; 1.
DR   PANTHER; PTHR30461:SF22; SERINE RECOMBINASE PINE-RELATED; 1.
DR   Pfam; PF02796; HTH_7; 1.
DR   Pfam; PF00239; Resolvase; 1.
DR   SMART; SM00857; Resolvase; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF53041; Resolvase-like; 1.
DR   PROSITE; PS00397; RECOMBINASES_1; 1.
DR   PROSITE; PS00398; RECOMBINASES_2; 1.
DR   PROSITE; PS51736; RECOMBINASES_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA integration; DNA recombination; DNA-binding; Plasmid;
KW   Transposable element.
FT   CHAIN           1..183
FT                   /note="Transposon gamma-delta resolvase"
FT                   /id="PRO_0000196367"
FT   DOMAIN          2..137
FT                   /note="Resolvase/invertase-type recombinase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01072"
FT   DNA_BIND        161..180
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        10
FT                   /note="O-(5'-phospho-DNA)-serine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01072,
FT                   ECO:0000269|PubMed:6099239"
FT   STRAND          3..11
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   HELIX           13..25
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1GDT"
FT   HELIX           46..54
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   HELIX           73..85
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   TURN            93..96
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   HELIX           102..127
FT                   /evidence="ECO:0007829|PDB:2GM5"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:1ZR4"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:1RES"
FT   HELIX           148..156
FT                   /evidence="ECO:0007829|PDB:1GDT"
FT   HELIX           161..168
FT                   /evidence="ECO:0007829|PDB:1GDT"
FT   HELIX           172..180
FT                   /evidence="ECO:0007829|PDB:1GDT"
SQ   SEQUENCE   183 AA;  20362 MW;  B2EBA6037F926FAB CRC64;
     MRLFGYARVS TSQQSLDIQV RALKDAGVKA NRIFTDKASG SSSDRKGLDL LRMKVEEGDV
     ILVKKLDRLG RDTADMIQLI KEFDAQGVSI RFIDDGISTD GEMGKMVVTI LSAVAQAERQ
     RILERTNEGR QEAMAKGVVF GRKRKIDRDA VLNMWQQGLG ASHISKTMNI ARSTVYKVIN
     ESN
//