TNSC_ECOLX
ID TNSC_ECOLX Reviewed; 555 AA.
AC P05846; Q7AJH6;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transposon Tn7 transposition protein TnsC;
DE Short=Protein E;
GN Name=tnsC;
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 1-294.
RX PubMed=3022239; DOI=10.1093/nar/14.20.7915;
RA Smith G.M., Jones P.;
RT "Tn7 transposition: a multigene process. Identification of a regulatory
RT gene product.";
RL Nucleic Acids Res. 14:7915-7927(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
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 [5]
RP ERRATUM OF PUBMED:1655576.
RA Orle K.A., Craig N.L.;
RL Gene 104:125-131(1991).
RN [6]
RP CHARACTERIZATION.
RX PubMed=1317955; DOI=10.1093/nar/20.10.2525;
RA Gamas P., Craig N.L.;
RT "Purification and characterization of TnsC, a Tn7 transposition protein
RT that binds ATP and DNA.";
RL Nucleic Acids Res. 20:2525-2532(1992).
RN [7] {ECO:0007744|PDB:1T0F}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 503-555, AND INTERACTION WITH
RP TNSA.
RX PubMed=15257292; DOI=10.1038/sj.emboj.7600311;
RA Ronning D.R., Li Y., Perez Z.N., Ross P.D., Hickman A.B., Craig N.L.,
RA Dyda F.;
RT "The carboxy-terminal portion of TnsC activates the Tn7 transposase through
RT a specific interaction with TnsA.";
RL EMBO J. 23:2972-2981(2004).
CC -!- FUNCTION: TnsC binds non-specifically to DNA in the presence of ATP. It
CC is required for Tn7 transposition.
CC -!- FUNCTION: TnsABC + TnsD promote high-frequency insertion of Tn7 into a
CC specific target site known as att-Tn7 whereas TnsABC + TnsE promote
CC low-frequency insertion into many different sites.
CC -!- SUBUNIT: Monomer. Interacts (via C-terminus) with TnsA; this
CC interaction allows TnsA to bind donor DNA (PubMed:15257292).
CC {ECO:0000269|PubMed:15257292}.
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DR EMBL; X17693; CAA35685.1; -; Genomic_DNA.
DR EMBL; AP002527; BAB12611.1; -; Genomic_DNA.
DR EMBL; X04492; CAA28180.1; -; Genomic_DNA.
DR EMBL; M37392; AAA24681.1; -; Genomic_DNA.
DR PIR; S12639; S12639.
DR RefSeq; NP_065318.1; NC_002525.1.
DR RefSeq; WP_001276994.1; NZ_WWEV01000116.1.
DR PDB; 1T0F; X-ray; 1.85 A; C/D=503-555.
DR PDB; 7MCS; EM; 3.56 A; A/B/C/D/E/F/G=1-503.
DR PDBsum; 1T0F; -.
DR PDBsum; 7MCS; -.
DR AlphaFoldDB; P05846; -.
DR SMR; P05846; -.
DR IntAct; P05846; 1.
DR PRIDE; P05846; -.
DR EvolutionaryTrace; P05846; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR021542; Tn7_TnsC.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF11426; Tn7_TnsC_Int; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA recombination; DNA-binding;
KW Nucleotide-binding; Plasmid; Transposable element; Transposition.
FT CHAIN 1..555
FT /note="Transposon Tn7 transposition protein TnsC"
FT /id="PRO_0000072613"
FT DNA_BIND 388..407
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 495..555
FT /note="Interaction with TnsA"
FT /evidence="ECO:0000269|PubMed:15257292"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:1T0F"
FT HELIX 521..526
FT /evidence="ECO:0007829|PDB:1T0F"
FT HELIX 534..540
FT /evidence="ECO:0007829|PDB:1T0F"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:1T0F"
SQ SEQUENCE 555 AA; 62995 MW; 3CDADC9C9BB5E135 CRC64;
MSATRIQAVY RDTGVEAYRD NPFIEALPPL QESVNSAASL KSSLQLTSSD LQKSRVIRAH
TICRIPDDYF QPLGTHLLLS ERISVMIRGG YVGRNPKTGD LQKHLQNGYE RVQTGELETF
RFEEARSTAQ SLLLIGCSGS GKTTSLHRIL ATYPQVIYHR ELNVEQVVYL KIDCSHNGSL
KEICLNFFRA LDRALGSNYE RRYGLKRHGI ETMLALMSQI ANAHALGLLV IDEIQHLSRS
RSGGSQEMLN FFVTMVNIIG VPVMLIGTPK AREIFEADLR SARRGAGFGA IFWDPIQQTQ
RGKPNQEWIA FTDNLWQLQL LQRKDALLSD EVRDVWYELS QGVMDIVVKL FVLAQLRALA
LGNERITAGL LRQVYQDELK PVHPMLEALR SGIPERIARY SDLVVPEIDK RLIQLQLDIA
AIQEQTPEEK ALQELDTEDQ RHLYLMLKED YDSSLLIPTI KKAFSQNPTM TRQKLLPLVL
QWLMEGETVV SELEKPSKSK KVSAIKVVKP SDWDSLPDTD LRYIYSQRQP EKTMHERLKG
KGVIVDMASL FKQAG