RAYT_ECOLI
ID RAYT_ECOLI Reviewed; 165 AA.
AC Q47152;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=REP-associated tyrosine transposase;
GN Name=rayT {ECO:0000303|PubMed:20085626};
GN Synonyms=TnpAREP {ECO:0000303|PubMed:22199259}, yafM;
GN OrderedLocusNames=b0228, JW0218;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7596361; DOI=10.1016/0165-7992(95)90024-1;
RA Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.;
RT "dinP, a new gene in Escherichia coli, whose product shows similarities to
RT UmuC and its homologues.";
RL Mutat. Res. 347:1-7(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, AND GENE NAME.
RX PubMed=20085626; DOI=10.1186/1471-2164-11-44;
RA Nunvar J., Huckova T., Licha I.;
RT "Identification and characterization of repetitive extragenic palindromes
RT (REP)-associated tyrosine transposases: implications for REP evolution and
RT dynamics in bacterial genomes.";
RL BMC Genomics 11:44-44(2010).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=22199259; DOI=10.1093/nar/gkr1198;
RA Ton-Hoang B., Siguier P., Quentin Y., Onillon S., Marty B., Fichant G.,
RA Chandler M.;
RT "Structuring the bacterial genome: Y1-transposases associated with REP-BIME
RT sequences.";
RL Nucleic Acids Res. 40:3596-3609(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=22885300; DOI=10.1093/nar/gks741;
RA Messing S.A., Ton-Hoang B., Hickman A.B., McCubbin A.J., Peaslee G.F.,
RA Ghirlando R., Chandler M., Dyda F.;
RT "The processing of repetitive extragenic palindromes: the structure of a
RT repetitive extragenic palindrome bound to its associated nuclease.";
RL Nucleic Acids Res. 40:9964-9979(2012).
CC -!- FUNCTION: Transposase that is always flanked by repeated extragenic
CC palindrome (REP) sequences, which are clustered in structures called
CC bacterial interspersed mosaic elements (BIMEs). RayT catalyzes cleavage
CC and recombination of BIMEs. Binds REP sequences and cleaves BIMEs both
CC upstream and downstream of the REP sequence. Could be important in the
CC creation of BIME variability and amplification.
CC {ECO:0000269|PubMed:20085626, ECO:0000269|PubMed:22199259,
CC ECO:0000269|PubMed:22885300}.
CC -!- ACTIVITY REGULATION: Cleavage occurs in the presence of magnesium, but
CC is much more pronounced with manganese. {ECO:0000269|PubMed:22199259}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22885300}.
CC -!- SIMILARITY: Belongs to the transposase 17 family. RAYT subfamily.
CC {ECO:0000305}.
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DR EMBL; D38582; BAA07590.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08648.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73332.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77898.1; -; Genomic_DNA.
DR PIR; E64747; E64747.
DR RefSeq; NP_414763.1; NC_000913.3.
DR RefSeq; WP_000006255.1; NZ_SSZK01000029.1.
DR PDB; 4ER8; X-ray; 2.60 A; A=1-165.
DR PDBsum; 4ER8; -.
DR AlphaFoldDB; Q47152; -.
DR SMR; Q47152; -.
DR BioGRID; 4259773; 31.
DR DIP; DIP-11217N; -.
DR IntAct; Q47152; 1.
DR STRING; 511145.b0228; -.
DR PaxDb; Q47152; -.
DR PRIDE; Q47152; -.
DR EnsemblBacteria; AAC73332; AAC73332; b0228.
DR EnsemblBacteria; BAA77898; BAA77898; BAA77898.
DR GeneID; 944913; -.
DR KEGG; ecj:JW0218; -.
DR KEGG; eco:b0228; -.
DR PATRIC; fig|1411691.4.peg.2055; -.
DR EchoBASE; EB2944; -.
DR eggNOG; COG1943; Bacteria.
DR HOGENOM; CLU_068226_6_0_6; -.
DR InParanoid; Q47152; -.
DR OMA; HVDYIHI; -.
DR PhylomeDB; Q47152; -.
DR BioCyc; EcoCyc:G6112-MON; -.
DR PRO; PR:Q47152; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000405; F:bubble DNA binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0032448; F:DNA hairpin binding; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0004803; F:transposase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IDA:EcoCyc.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro.
DR Gene3D; 3.30.70.1290; -; 1.
DR InterPro; IPR002686; Transposase_17.
DR InterPro; IPR036515; Transposase_17_sf.
DR SMART; SM01321; Y1_Tnp; 1.
DR SUPFAM; SSF143422; SSF143422; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Manganese; Reference proteome;
KW Transposable element; Transposition.
FT CHAIN 1..165
FT /note="REP-associated tyrosine transposase"
FT /id="PRO_0000168536"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:4ER8"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4ER8"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:4ER8"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4ER8"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:4ER8"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:4ER8"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4ER8"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:4ER8"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4ER8"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4ER8"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:4ER8"
SQ SEQUENCE 165 AA; 20042 MW; 970463B76841B864 CRC64;
MSEYRRYYIK GGTWFFTVNL RNRRSQLLTT QYQMLRHAII KVKRDRPFEI NAWVVLPEHM
HCIWTLPEGD DDFSSRWREI KKQFTHACGL KNIWQPRFWE HAIRNTKDYR HHVDYIYINP
VKHGWVKQVS DWPFSTFHRD VARGLYPIDW AGDVTDFSAG ERIIS
