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   24-JAN-2024, entry version 98.
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; Pseudomonadota; 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:InterPro.
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   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 6.10.140.290; -; 1.
DR   Gene3D; 6.10.250.110; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR014129; Conjug_relaxase_TraI.
DR   InterPro; IPR009767; DNA_helicase_TraI_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014059; TraI/TrwC_relax.
DR   InterPro; IPR040668; TraI_2B.
DR   InterPro; IPR040987; TraI_N.
DR   InterPro; IPR014862; TrwC.
DR   NCBIfam; NF041492; MobF; 1.
DR   NCBIfam; TIGR02686; relax_trwC; 1.
DR   NCBIfam; TIGR02760; TraI_TIGR; 1.
DR   Pfam; PF13604; AAA_30; 1.
DR   Pfam; PF18272; ssDNA_TraI_N; 1.
DR   Pfam; PF18340; TraI_2B; 1.
DR   Pfam; PF07057; TraI_C; 1.
DR   Pfam; PF08751; TrwC; 1.
DR   SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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
//