TRAI2_ECOLX
ID TRAI2_ECOLX Reviewed; 1756 AA.
AC P22706; Q51812;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Multifunctional conjugation protein TraI;
DE Includes:
DE RecName: Full=DNA relaxase TraI;
DE EC=5.6.2.1;
DE AltName: Full=DNA nickase TraI;
DE AltName: Full=Transesterase TraI;
DE Includes:
DE RecName: Full=DNA helicase I;
DE EC=3.6.4.12;
GN Name=traI;
OS Escherichia coli.
OG Plasmid IncFII R100 (NR1), Plasmid F, and Plasmid R6-5.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncFII R100 (NR1);
RX PubMed=2164585; DOI=10.1016/0022-2836(90)90145-c;
RA Yoshioka Y., Fujita Y., Ohtsubo E.;
RT "Nucleotide sequence of the promoter-distal region of the tra operon of
RT plasmid R100, including traI (DNA helicase I) and traD genes.";
RL J. Mol. Biol. 214:39-53(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1747-1756.
RC PLASMID=F, and R6-5;
RX PubMed=1916281; DOI=10.1016/0378-1119(91)90469-r;
RA Cram D.S., Loh S.M., Cheah K.C., Skurray R.A.;
RT "Sequence and conservation of genes at the distal end of the transfer
RT region on plasmids F and R6-5.";
RL Gene 104:85-90(1991).
CC -!- FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer
CC of ssDNA plasmid from a donor to a recipient cell. It is the central
CC mechanism by which antibiotic resistance and virulence factors are
CC propagated in bacterial populations. Part of the relaxosome, which
CC facilitates a site- and strand-specific cut in the origin of transfer
CC by TraI, at the nic site. Relaxosome formation requires binding of IHF
CC and TraY to the oriT region, which then facilitates binding of TraI
CC relaxase. TraI forms a covalent 5'-phosphotyrosine intermediate linkage
CC to the ssDNA. The transesterified T-strand moves from the donor cell to
CC the recipient cell in a 5'to 3' direction, with the DNA helicase
CC activity of TraI unwinding the DNA. DNA transfer occurs via the
CC conjugative pore (transferosome) an intercellular junction mediated by
CC a type IV secretion system, with TraD providing the means to link the
CC relaxosome to the conjugative pore. The relaxase completes DNA transfer
CC by reversing the covalent phosphotyrosine linkage and releasing the T-
CC strand.
CC -!- FUNCTION: TraI has also been identified as DNA helicase I. DNA.
CC helicase I is a potent, highly processive DNA-dependent ATPase, able to
CC unwind about 1.1 kb dsDNA per second in a 5' to 3' manner (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. Part of the relaxosome, a complex composed of
CC plasmid-encodes TraI, TraM, TraY and host-encoded IHF bound to the F
CC plasmid origin of transfer (oriT). Directly contacts coupling protein
CC TraD. Seems to directly contact TraM via its C-terminus.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: To TraI of plasmid F. {ECO:0000305}.
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DR EMBL; X55815; CAA39337.1; -; Genomic_DNA.
DR EMBL; M38047; AAA98090.1; -; Genomic_DNA.
DR PIR; S10660; BVECAI.
DR AlphaFoldDB; P22706; -.
DR SMR; P22706; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014059; Conjug_relaxase_N.
DR InterPro; IPR014129; Conjug_relaxase_TraI.
DR InterPro; IPR009767; DNA_helicase_TraI.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040668; TraI_2B.
DR InterPro; IPR040987; TraI_N.
DR InterPro; IPR014862; TrwC.
DR Pfam; PF18272; ssDNA_TraI_N; 1.
DR Pfam; PF07057; TraI; 1.
DR Pfam; PF18340; TraI_2B; 1.
DR Pfam; PF08751; TrwC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR02686; relax_trwC; 1.
DR TIGRFAMs; TIGR02760; TraI_TIGR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Conjugation; Cytoplasm; DNA-binding; Helicase;
KW Hydrolase; Isomerase; Magnesium; Metal-binding; Mobility protein;
KW Multifunctional enzyme; Nucleotide-binding; Plasmid.
FT CHAIN 1..1756
FT /note="Multifunctional conjugation protein TraI"
FT /id="PRO_0000068453"
FT REGION 1..330
FT /note="DNA relaxase"
FT REGION 950..1500
FT /note="DNA helicase I"
FT COILED 1719..1753
FT /evidence="ECO:0000255"
FT ACT_SITE 16
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate; for
FT relaxase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 17
FT /note="Relaxase"
FT /evidence="ECO:0000255"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 992..999
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1756 AA; 191681 MW; B394B666141153F3 CRC64;
MLSFSVVKSA GSAGNYYTDK DNYYVLGSMG ERWAGQGAEQ LGLQGSVDKD VFTRLLEGRL
PDGADLSRMQ DGSNKHRPGY DLTFSAPKSV SMMAMLGGDK RLIDAHNQAV DFAVRQVEAL
ASTRVMTDGQ SETVLTGNLV MALFNHDTSR DQDPQLHTHV VVANVTQHNG EWKTLSSDKV
GKTGFSENVL ANRIAFGKIY QSELRQRVEA LGYETEVVGK HGMWEMPGVP VEAFSSRSQA
IREAVGEDAS LKSRDVAALD TRKSKHHVDP EVRMAEWMQT LKETGFDIRA YRDAADQRAE
IRTQAPGPAS QDGPDVQQAV TQAIAGLSER KVQFTYTDVL ARTVGILPPE NGVIERARAG
IDEAISREQL IPLDREKGLF TSGIHVLDEL SVRALSRDIM KQNRVTVHPE KSVPRTAGYS
DAVSVLAQDR PSLAIVSGQG GAAGQRERVA ELVMMAREQG REVQIIAADR RSQLNLKQDE
RLSGELITGR RQLQEGMVFT SGSTFIVDQG EKLSLKETLT LLDGAARHNV QVLITDSGQR
TGTGSALMAM KDAGVNTYRW QGGEQRPATI ISEPDRNVRY DRLAGDFAAS VKAGEESVAQ
VSGVREQAIL TQAIRSELKT QGVLGHPEVT MTALSPVWLD SRSRYLRDMY RPGMVMEQWN
PETRSHDRYV IDRVTAQSHS LTLRDAQGET QVVRISSLDS SWSLFRPEKM PVADGERLRV
TGKIPGLRVS GGDRLQVASV SEDAMTVVVP GRAEPATLPV ADSPFTALKL ENGWVETPGH
SVSDSATVFA SVTQMAMDNA TLNGLARSGR DVRLYSSLDE TRTAEKLARH PSFTVVSEQI
KARAGETSLE TAISLQKTGL HTPAQQAIHL ALPVLESKNL AFSMVDLLTE AKSFAAEGTG
FTELGGEINA QIKRGDLLYV DVAKGYGTGL LVSRASYEAE KSILRHILEG KEAVTPLMER
VPGELMETLT SGPRAATRMI LETSDRFTVV QGYAGVGKTT QFRAVMSAVN MLPASERPRV
VGLGPTHRAV GEMRSAGVDA QTLASFLHDT QLQQRSGETP DFSNTLFLLD ESSMVGNTDM
ARAYALIAAG GGRAVASGDT DQLQAIAPGQ PFRLQQTRSA ADVVIMKEIV RQTPELREAV
YSLINRDVER ALSGLESVKP SQVPRQEGAW APEHSVTEFS HSQEAKLAEA QQKAMLKGET
FPDVPMTLYE AIVRDYTGRT PEAREQTLIV THLNEDRRVL NSMIHDAREK AGELGKEQVM
VPVLNTANIR DGELRRLSTW ENNPDALALV DSVYHRIAGI SKDDGLITLE DAEGNTRLIS
PREAVAEGVT LYTPDKIRVG TGDRMRFTKS DRERGYVANS VWTVTAVSGD SVTLSDGQQT
RVIRPGQERA EQHIDLAYAI TAHGAQGASE TFAIALEGTE GNRKLMAGFE SAYVALSRMK
QHVQVYTDNR QGWTDAINNA VQKGTAHDVL EPKPDREVMN AQRLFSTARE LRDVAAGRAV
LRQAGLAGGD SPARFIAPGR KYPQPYVALP AFDRNGKSAG IWLNPLTTDD GNGLRGFSGE
GRVKGSGDAQ FVALQGSRNG ESLLADNMQD GVRIARDNPD SGVVVRIAGE GRPWNPGAIT
GGRVWGDIPD SSVQPGAGNG EPVTAEVLAQ RQAEEAIRRE TERRADEIVR KMAENKPDLP
DGKTEQAVRE IAGQERDRAD ITEREAALPE SVLRESQREQ EAVREVAREN LLQERLQQIE
RDMVRDLQKE KTLGGD
