TNSB_ECOLX
ID TNSB_ECOLX Reviewed; 702 AA.
AC P13989; Q9R5R8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Transposon Tn7 transposition protein TnsB;
GN Name=tnsB;
OS Escherichia coli.
OG Plasmid R721.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2156235; DOI=10.1093/nar/18.4.901;
RA Flores C., Qadri M.I., Lichtenstein C.;
RT "DNA sequence analysis of five genes; tnsA, B, C, D and E, required for Tn7
RT transposition.";
RL Nucleic Acids Res. 18:901-911(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=R721;
RA Sampei G., Motomura K., Masuda S., Yamaguchi T., Ando K., Oishi T.,
RA Furuya N., Komano T., Mizobuchi K.;
RT "Organization and diversification of plasmid genomes: complete nucleotide
RT sequence of the R721 genome.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
RX PubMed=1655576; DOI=10.1016/0378-1119(91)90478-t;
RA Orle K.A., Craig N.L.;
RT "Identification of transposition proteins encoded by the bacterial
RT transposon Tn7.";
RL Gene 96:1-7(1990).
RN [4]
RP ERRATUM OF PUBMED:1655576.
RA Orle K.A., Craig N.L.;
RL Gene 104:125-131(1991).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RX PubMed=1657979; DOI=10.1016/s0021-9258(18)54698-6;
RA Arciszewska L.K., McKown R.L., Craig N.L.;
RT "Purification of TnsB, a transposition protein that binds to the ends of
RT Tn7.";
RL J. Biol. Chem. 266:21736-21744(1991).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ASP-273; ASP-278; ASP-283; ASP-301; SER-304;
RP ASP-361; GLU-364; GLU-371; GLU-396 AND GLU-424.
RX PubMed=8947057; DOI=10.1002/j.1460-2075.1996.tb01024.x;
RA Sarnovsky R.J., May E.W., Craig N.L.;
RT "The Tn7 transposase is a heteromeric complex in which DNA breakage and
RT joining activities are distributed between different gene products.";
RL EMBO J. 15:6348-6361(1996).
RN [7]
RP FUNCTION.
RX PubMed=10704304; DOI=10.1006/jmbi.2000.3558;
RA Biery M.C., Lopata M., Craig N.L.;
RT "A minimal system for Tn7 transposition: the transposon-encoded proteins
RT TnsA and TnsB can execute DNA breakage and joining reactions that generate
RT circularized Tn7 species.";
RL J. Mol. Biol. 297:25-37(2000).
CC -!- FUNCTION: Sequence-specific, DNA-binding protein required for Tn7
CC transposition. Recognizes sequences necessary for recombination at both
CC left and right ends of Tn7 and, together with TnsA, forms the
CC transposase. TnsB executes the 5'-DNA strand breakage and joining
CC reactions. {ECO:0000269|PubMed:10704304, ECO:0000269|PubMed:8947057}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17693; CAA35684.1; -; Genomic_DNA.
DR EMBL; AP002527; BAB12612.1; -; Genomic_DNA.
DR PIR; S12638; S12638.
DR RefSeq; NP_065319.1; NC_002525.1.
DR RefSeq; WP_000267723.1; NZ_WWEV01000116.1.
DR AlphaFoldDB; P13989; -.
DR BRENDA; 2.7.7.B22; 2026.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004803; F:transposase activity; IDA:UniProtKB.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006313; P:transposition, DNA-mediated; IDA:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00665; rve; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA recombination; DNA-binding; Plasmid;
KW Transposable element; Transposition.
FT CHAIN 1..702
FT /note="Transposon Tn7 transposition protein TnsB"
FT /id="PRO_0000072612"
FT DOMAIN 262..480
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT DNA_BIND 105..124
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 137..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 273
FT /note="D->N: Prevents DNA strand breakage and joining
FT reactions."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 278
FT /note="D->N: No effect on recombination."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 283
FT /note="D->N: No effect on recombination."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 301
FT /note="D->A: Prevents DNA strand breakage and joining
FT reactions."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 304
FT /note="S->A: No effect on recombination."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 361
FT /note="D->N: Prevents DNA strand breakage and joining
FT reactions."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 364
FT /note="E->A: DNA strand single-end joining."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 371
FT /note="E->A: No effect on recombination."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 396
FT /note="E->Q: Prevents DNA strand breakage and joining
FT reactions."
FT /evidence="ECO:0000269|PubMed:8947057"
FT MUTAGEN 424
FT /note="E->A: No effect on recombination."
FT /evidence="ECO:0000269|PubMed:8947057"
SQ SEQUENCE 702 AA; 80825 MW; C71AE57F2DA1B0D8 CRC64;
MWQINEVVLF DNDPYRILAI EDGQVVWMQI SADKGVPQAR AELLLMQYLD EGRLVRTDDP
YVHLDLEEPS VDSVSFQKRE EDYRKILPII NSKDRFDPKV RSELVEHVVQ EHKVTKATVY
KLLRRYWQRG QTPNALIPDY KNSGAPGERR SATGTAKIGR AREYGKGEGT KVTPEIERLF
RLTIEKHLLN QKGTKTTVAY RRFVDLFAQY FPRIPQEDYP TLRQFRYFYD REYPKAQRLK
SRVKAGVYKK DVRPLSSTAT SQALGPGSRY EIDATIADIY LVDHHDRQKI IGRPTLYIVI
DVFSRMITGF YIGFENPSYV VAMQAFVNAC SDKTAICAQH DIEISSSDWP CVGLPDVLLA
DRGELMSHQV EALVSSFNVR VESAPPRRGD AKGIVESTFR TLQAEFKSFA PGIVEGSRIK
SHGETDYRLD ASLSVFEFTQ IILRTILFRN NHLVMDKYDR DADFPTDLPS IPVQLWQWGM
QHRTGSLRAV EQEQLRVALL PRRKVSISSF GVNLWGLYYS GSEILREGWL QRSTDIARPQ
HLEAAYDPVL VDTIYLFPQV GSRVFWRCNL TERSRQFKGL SFWEVWDIQA QEKHNKANAK
QDELTKRREL EAFIQQTIQK ANKLTPSTTE PKSTRIKQIK TNKKEAVTSE RKKRAEHLKP
SSSGDEAKVI PFNAVEADDQ EDYSLPTYVP ELFQDPPEKD ES