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P14565

- TRAI1_ECOLI

UniProt

P14565 - TRAI1_ECOLI

Protein

Multifunctional conjugation protein TraI

Gene

traI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then faciliates binding of TraI relaxase. TraI forms a covalent 5'-phosphotyrosine intermediate linkage to the ssDNA. The transesterified T-strand moves from the donor cell to the recipient cell in a 5'to 3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the conjugative pore (transferosome) an intercellular junction mediated by a type IV secretion system, with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage and releasing the T-strand.
    TraI has also been identified as DNA helicase I. DNA. helicase I is a potent, highly processive DNA-dependent ATPase, able to unwind about 1.1 kb dsDNA per second in a 5' to 3' manner.

    Catalytic activityi

    ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
    ATP + H2O = ADP + phosphate.

    Cofactori

    Mg2+.

    Enzyme regulationi

    Nicking activity (relaxase) is inhibited by bisphosphonates such as the non-competitive inhibitor imidobisphosphate (PNP), etidronic acid (ETIDRO) and clodronic acid (CLODRO). The latter 2 are competitive inhibitors, and are already used clinically to treat bone loss (marketed as Didronel and Bonefos). All 3 compounds also inhibit conjugation and kill F plasmid-containing cells. They are specific to dual tyrosine relaxases such as those found in F and related R conjugative plasmids.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei16 – 161O-(5'-phospho-DNA)-tyrosine intermediate; for relaxase activityCurated
    Active sitei17 – 171RelaxaseSequence Analysis
    Metal bindingi146 – 1461Magnesium; via pros nitrogen; catalytic1 Publication
    Metal bindingi157 – 1571Magnesium; via tele nitrogen; catalytic1 Publication
    Metal bindingi159 – 1591Magnesium; via tele nitrogen; catalytic1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi992 – 9998ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA helicase activity Source: InterPro
    4. DNA topoisomerase type I activity Source: UniProtKB-EC
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. conjugation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Isomerase, Mobility protein

    Keywords - Biological processi

    Conjugation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multifunctional conjugation protein TraI
    Including the following 2 domains:
    DNA relaxase TraI (EC:5.99.1.2)
    Alternative name(s):
    DNA nickase TraI
    Transesterase TraI
    DNA helicase I (EC:3.6.4.12)
    Gene namesi
    Name:traI
    Ordered Locus Names:ECOK12F104
    Encoded oniPlasmid F20 Publications
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Loss of conjugative DNA transfer.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 11Missing: Loss of ssDNA binding. 1 Publication
    Mutagenesisi3 – 31S → A: 1000-fold reduced affinity for ssDNA. 1 Publication
    Mutagenesisi16 – 161Y → F: Loss of DNA nicking ability; still binds ssDNA. 3 Publications
    Mutagenesisi17 – 171Y → F: Loss of DNA nicking ability; still binds ssDNA. 1 Publication
    Mutagenesisi23 – 231Y → F: Reduced DNA nicking ability. 1 Publication
    Mutagenesisi24 – 241Y → F: Reduced DNA nicking ability. 1 Publication
    Mutagenesisi88 – 881K → A: 10000-fold reduced affinity for ssDNA. 1 Publication
    Mutagenesisi159 – 1591H → E: Loss of oriT cleavage. 1 Publication
    Mutagenesisi237 – 2371R → A: 300-fold reduced affinity for ssDNA. 1 Publication
    Mutagenesisi241 – 2411I → A: 1500-fold reduced affinity for ssDNA. 1 Publication
    Mutagenesisi998 – 9981K → M: No helicase activity, nicks DNA, loss of DNA transfer activity. 2 Publications
    Mutagenesisi1517 – 15259Missing: 10,000-fold reduction in conjugative DNA transfer.
    Mutagenesisi1518 – 15258PGRKYPQP → GGRKYGQG: 100,000-fold reduction in conjugative DNA transfer.
    Mutagenesisi1574 – 15752LQ → AA: 200-fold reduction in conjugative DNA transfer; when associated with A-1603.
    Mutagenesisi1603 – 16031V → A: 200-fold reduction in conjugative DNA transfer; when associated with 1574-A-A-1575. 1 Publication
    Mutagenesisi1721 – 175636Missing: More than 100-fold reduction in conjugative DNA transfer. Add
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17561756Multifunctional conjugation protein TraIPRO_0000024504Add
    BLAST

    Proteomic databases

    PRIDEiP14565.

    Expressioni

    Gene expression databases

    GenevestigatoriP14565.

    Interactioni

    Subunit structurei

    Monomer. Part of the relaxosome, a complex composed of plasmid-encodes TraI, TraM, TraY and host-encoded IHF bound to the F plasmid origin of transfer (oriT). Directly contacts coupling protein TraD. Seems to directly contact TraM via its C-terminus.5 Publications

    Structurei

    Secondary structure

    1
    1756
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi10 – 178
    Helixi20 – 223
    Turni24 – 263
    Beta strandi32 – 354
    Helixi36 – 416
    Helixi49 – 568
    Beta strandi61 – 633
    Turni71 – 733
    Beta strandi79 – 857
    Helixi88 – 958
    Helixi101 – 11818
    Beta strandi122 – 1243
    Beta strandi133 – 1353
    Beta strandi141 – 1488
    Beta strandi154 – 16411
    Beta strandi166 – 1683
    Beta strandi171 – 1733
    Turni179 – 1813
    Helixi185 – 1906
    Helixi193 – 21018
    Helixi220 – 2223
    Helixi231 – 2344
    Helixi236 – 2449
    Helixi251 – 26010
    Helixi270 – 28213
    Turni283 – 2853
    Helixi288 – 2969
    Helixi390 – 40314
    Helixi409 – 4113
    Helixi417 – 42913
    Helixi443 – 45816
    Beta strandi463 – 4664
    Helixi471 – 4766
    Turni479 – 4813
    Beta strandi486 – 4883
    Turni489 – 4957
    Beta strandi504 – 5129
    Helixi513 – 52715
    Beta strandi532 – 5387
    Turni539 – 5413
    Helixi544 – 5529
    Helixi1477 – 148711
    Helixi1491 – 14933
    Helixi1495 – 150410
    Beta strandi1514 – 15163
    Beta strandi1526 – 15327
    Beta strandi1538 – 15458
    Beta strandi1547 – 15493
    Turni1550 – 15523
    Beta strandi1553 – 15553
    Beta strandi1562 – 15654
    Beta strandi1571 – 15766
    Beta strandi1578 – 158710
    Helixi1588 – 159710
    Beta strandi1601 – 16088
    Helixi1616 – 16183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P4DX-ray2.60A/B/C1-330[»]
    2A0IX-ray2.72A1-330[»]
    2L8BNMR-A381-569[»]
    2Q7TX-ray2.42A/B1-300[»]
    2Q7UX-ray3.00A/B1-300[»]
    3FLDX-ray2.40A/B1476-1628[»]
    ProteinModelPortaliP14565.
    SMRiP14565. Positions 1-306, 962-1033, 1398-1448, 1476-1628.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14565.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 330330DNA relaxaseAdd
    BLAST
    Regioni950 – 1500551DNA helicase IAdd
    BLAST
    Regioni1534 – 1756223Required for DNA transfer, may interact with TraMAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1717 – 175337Sequence AnalysisAdd
    BLAST

    Domaini

    Has 4 domains; the relaxase domain (residues 1-330), an unknown domain (residues 330-990), the helicase domain (residues 990-1450) and the C-terminal domain (1450-1756) which is required for conjugative DNA transfer, possibly via interaction with TraM.2 Publications

    Sequence similaritiesi

    To TraI of plasmid IncFII R100.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    OMAiETHRDAL.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR014059. Conjug_relaxase_N.
    IPR014129. Conjug_relaxase_TraI.
    IPR009767. DNA_helicase_TraI.
    IPR027417. P-loop_NTPase.
    IPR014862. TrwC.
    [Graphical view]
    PfamiPF07057. TraI. 1 hit.
    PF08751. TrwC. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    TIGRFAMsiTIGR02686. relax_trwC. 1 hit.
    TIGR02760. TraI_TIGR. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform traI (identifier: P14565-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMSIAQVRSA GSAGNYYTDK DNYYVLGSMG ERWAGRGAEQ LGLQGSVDKD     50
    VFTRLLEGRL PDGADLSRMQ DGSNRHRPGY DLTFSAPKSV SMMAMLGGDK 100
    RLIDAHNQAV DFAVRQVEAL ASTRVMTDGQ SETVLTGNLV MALFNHDTSR 150
    DQEPQLHTHA VVANVTQHNG EWKTLSSDKV GKTGFIENVY ANQIAFGRLY 200
    REKLKEQVEA LGYETEVVGK HGMWEMPGVP VEAFSGRSQT IREAVGEDAS 250
    LKSRDVAALD TRKSKQHVDP EIKMAEWMQT LKETGFDIRA YRDAADQRAD 300
    LRTLTPGPAS QDGPDVQQAV TQAIAGLSER KVQFTYTDVL ARTVGILPPE 350
    NGVIERARAG IDEAISREQL IPLDREKGLF TSGIHVLDEL SVRALSRDIM 400
    KQNRVTVHPE KSVPRTAGYS DAVSVLAQDR PSLAIVSGQG GAAGQRERVA 450
    ELVMMAREQG REVQIIAADR RSQMNMKQDE RLSGELITGR RQLLEGMAFT 500
    PGSTVIVDQG EKLSLKETLT LLDGAARHNV QVLITDSGQR TGTGSALMAM 550
    KDAGVNTYRW QGGEQRPATI ISEPDRNVRY ARLAGDFAAS VKAGEESVAQ 600
    VSGVREQAIL TQAIRSELKT QGVLGLPEVT MTALSPVWLD SRSRYLRDMY 650
    RPGMVMEQWN PETRSHDRYV IDRVTAQSHS LTLRDAQGET QVVRISSLDS 700
    SWSLFRPEKM PVADGERLRV TGKIPGLRVS GGDRLQVASV SEDAMTVVVP 750
    GRAEPATLPV SDSPFTALKL ENGWVETPGH SVSDSATVFA SVTQMAMDNA 800
    TLNGLARSGR DVRLYSSLDE TRTAEKLARH PSFTVVSEQI KTRAGETSLE 850
    TAISHQKSAL HTPAQQAIHL ALPVVESKKL AFSMVDLLTE AKSFAAEGTG 900
    FTELGGEINA QIKRGDLLYV DVAKGYGTGL LVSRASYEAE KSILRHILEG 950
    KEAVMPLMER VPGELMEKLT SGQRAATRMI LETSDRFTVV QGYAGVGKTT 1000
    QFRAVMSAVN MLPESERPRV VGLGPTHRAV GEMRSAGVDA QTLASFLHDT 1050
    QLQQRSGETP DFSNTLFLLD ESSMVGNTDM ARAYALIAAG GGRAVASGDT 1100
    DQLQAIAPGQ PFRLQQTRSA ADVAIMKEIV RQTPELREAV YSLINRDVER 1150
    ALSGLESVKP SQVPRQEGAW APEHSVTEFS HSQEAKLAEA QQKAMLKGEA 1200
    FPDVPMTLYE AIVRDYTGRT PEAREQTLIV THLNEDRRVL NSMIHDVREK 1250
    AGELGKEQVM VPVLNTANIR DGELRRLSTW ETHRDALVLV DNVYHRIAGI 1300
    SKDDGLITLQ DAEGNTRLIS PREAVAEGVT LYTPDTIRVG TGDRMRFTKS 1350
    DRERGYVANS VWTVTAVSGD SVTLSDGQQT REIRPGQEQA EQHIDLAYAI 1400
    TAHGAQGASE TFAIALEGTE GNRKLMAGFE SAYVALSRMK QHVQVYTDNR 1450
    QGWTDAINNA VQKGTAHDVF EPKPDREVMN AERLFSTARE LRDVAAGRAV 1500
    LRQAGLAGGD SPARFIAPGR KYPQPYVALP AFDRNGKSAG IWLNPLTTDD 1550
    GNGLRGFSGE GRVKGSGDAQ FVALQGSRNG ESLLADNMQD GVRIARDNPD 1600
    SGVVVRIAGE GRPWNPGAIT GGRVWGDIPD NSVQPGAGNG EPVTAEVLAQ 1650
    RQAEEAIRRE TERRADEIVR KMAENKPDLP DGKTEQAVRE IAGQERDRAA 1700
    ITEREAALPE GVLREPQRVR EAVREIAREN LLQERLQQME RDMVRDLQKE 1750
    KTLGGD 1756
    Length:1,756
    Mass (Da):192,016
    Last modified:November 1, 1990 - v2
    Checksum:iAA07D61DB2BFD9FA
    GO
    Isoform traI* (identifier: P14565-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-954: Missing.

    Show »
    Length:802
    Mass (Da):87,882
    Checksum:iED17E7673621E2EF
    GO

    Sequence cautioni

    The sequence AAA83930.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 746MQDGSN → CRMAVT in AAA83930. (PubMed:2680768)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 954954Missing in isoform traI*. CuratedVSP_018971Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M54796 Genomic DNA. Translation: AAA98085.1.
    M54796 Genomic DNA. Translation: AAA98086.1.
    U01159 Genomic DNA. Translation: AAC44186.1.
    AP001918 Genomic DNA. Translation: BAA97974.1.
    M29254 Genomic DNA. Translation: AAA83930.1. Different initiation.
    X57430 Genomic DNA. Translation: CAA40677.1.
    U01159 Genomic DNA. Translation: AAC44187.1.
    RefSeqiNP_061483.1. NC_002483.1. [P14565-1]
    WP_000987005.1. NC_002483.1.

    Genome annotation databases

    GeneIDi1263574.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M54796 Genomic DNA. Translation: AAA98085.1 .
    M54796 Genomic DNA. Translation: AAA98086.1 .
    U01159 Genomic DNA. Translation: AAC44186.1 .
    AP001918 Genomic DNA. Translation: BAA97974.1 .
    M29254 Genomic DNA. Translation: AAA83930.1 . Different initiation.
    X57430 Genomic DNA. Translation: CAA40677.1 .
    U01159 Genomic DNA. Translation: AAC44187.1 .
    RefSeqi NP_061483.1. NC_002483.1. [P14565-1 ]
    WP_000987005.1. NC_002483.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P4D X-ray 2.60 A/B/C 1-330 [» ]
    2A0I X-ray 2.72 A 1-330 [» ]
    2L8B NMR - A 381-569 [» ]
    2Q7T X-ray 2.42 A/B 1-300 [» ]
    2Q7U X-ray 3.00 A/B 1-300 [» ]
    3FLD X-ray 2.40 A/B 1476-1628 [» ]
    ProteinModelPortali P14565.
    SMRi P14565. Positions 1-306, 962-1033, 1398-1448, 1476-1628.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P14565.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1263574.

    Phylogenomic databases

    OMAi ETHRDAL.

    Miscellaneous databases

    EvolutionaryTracei P14565.
    PROi P14565.

    Gene expression databases

    Genevestigatori P14565.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR014059. Conjug_relaxase_N.
    IPR014129. Conjug_relaxase_TraI.
    IPR009767. DNA_helicase_TraI.
    IPR027417. P-loop_NTPase.
    IPR014862. TrwC.
    [Graphical view ]
    Pfami PF07057. TraI. 1 hit.
    PF08751. TrwC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    TIGRFAMsi TIGR02686. relax_trwC. 1 hit.
    TIGR02760. TraI_TIGR. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the traI (helicase I) gene from the sex factor F."
      Bradshaw H.D. Jr., Traxler B.A., Minkley E.G. Jr., Nester E.W., Gordon M.P.
      J. Bacteriol. 172:4127-4131(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Plasmid: F
    2. "Analysis of the sequence and gene products of the transfer region of the F sex factor."
      Frost L.S., Ippen-Ihler K., Skurray R.A.
      Microbiol. Rev. 58:162-210(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Plasmid: F
    3. "Complete nucleotide sequence of the F plasmid: its implications for organization and diversification of plasmid genomes."
      Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / CR63.
      Plasmid: F
    4. "Nucleotide sequence of the traD region in the Escherichia coli F sex factor."
      Jalajakumari M.B., Manning P.A.
      Gene 81:195-202(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
      Strain: K12.
      Plasmid: F
    5. "Nucleotide sequence of the promoter-distal region of the tra operon of plasmid R100, including traI (DNA helicase I) and traD genes."
      Yoshioka Y., Fujita Y., Ohtsubo E.
      J. Mol. Biol. 214:39-53(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
      Plasmid: F
    6. "Subdomain organization and catalytic residues of the F factor TraI relaxase domain."
      Street L.M., Harley M.J., Stern J.C., Larkin C., Williams S.L., Miller D.L., Dohm J.A., Rodgers M.E., Schildbach J.F.
      Biochim. Biophys. Acta 1646:86-99(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5, FUNCTION IN SS-DNA DIGESTION, SUBUNIT, CHARACTERIZATION OF RELAXASE CATALYTIC RESIDUES, MUTAGENESIS OF TYR-16; TYR-17; TYR-23 AND TYR-24.
      Plasmid: F
    7. "Regulation of the expression of the traM gene of the F sex factor of Escherichia coli."
      Penfold S.S., Simon J., Frost L.S.
      Mol. Microbiol. 20:549-558(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-1756.
      Plasmid: F
    8. "Identification of Escherichia coli DNA helicase I as the traI gene product of the F sex factor."
      Abdel-Monem M., Taucher-Scholz G., Klinkert M.Q.
      Proc. Natl. Acad. Sci. U.S.A. 80:4659-4663(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS DNA HELICASE I.
      Plasmid: F
    9. "Characterization of the reaction product of the oriT nicking reaction catalyzed by Escherichia coli DNA helicase I."
      Matson S.W., Nelson W.C., Morton B.S.
      J. Bacteriol. 175:2599-2606(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN COVALENT BINDING TO SS-DNA.
      Plasmid: F
    10. "The traY gene product and integration host factor stimulate Escherichia coli DNA helicase I-catalyzed nicking at the F plasmid oriT."
      Nelson W.C., Howard M.T., Sherman J.A., Matson S.W.
      J. Biol. Chem. 270:28374-28380(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN F PLASMID NICKING.
      Plasmid: F
    11. "Stepwise assembly of a relaxosome at the F plasmid origin of transfer."
      Howard M.T., Nelson W.C., Matson S.W.
      J. Biol. Chem. 270:28381-28386(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF RELAXOSOME ASSEMBLY ORDER.
      Plasmid: F
    12. "DNA recognition by F factor TraI36: highly sequence-specific binding of single-stranded DNA."
      Stern J.C., Schildbach J.F.
      Biochemistry 40:11586-11595(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SS-DNA-BINDING, CHARACTERIZATION OF DNA SEQUENCE SPECIFICITY, MUTAGENESIS OF TYR-16.
      Plasmid: F
    13. "F plasmid conjugative DNA transfer: the TraI helicase activity is essential for DNA strand transfer."
      Matson S.W., Sampson J.K., Byrd D.R.
      J. Biol. Chem. 276:2372-2379(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-998.
      Plasmid: F
    14. "The F-plasmid TraI protein contains three functional domains required for conjugative DNA strand transfer."
      Matson S.W., Ragonese H.
      J. Bacteriol. 187:697-706(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE C-TERMINUS, DOMAINS, MUTAGENESIS OF LYS-998.
      Plasmid: F
    15. "DNA unwinding by Escherichia coli DNA helicase I (TraI) provides evidence for a processive monomeric molecular motor."
      Sikora B., Eoff R.L., Matson S.W., Raney K.D.
      J. Biol. Chem. 281:36110-36116(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF HELICASE ACTIVITY, SUBUNIT.
      Plasmid: F
    16. "The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage at oriT through an interaction with TraI."
      Ragonese H., Haisch D., Villareal E., Choi J.H., Matson S.W.
      Mol. Microbiol. 63:1173-1184(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAM; TRAY AND IHF, SUBUNIT.
      Plasmid: F
    17. "Structural insights into single-stranded DNA binding and cleavage by F factor TraI."
      Datta S., Larkin C., Schildbach J.F.
      Structure 11:1369-1379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-330 IN COMPLEX WITH MAGNESIUM.
      Plasmid: F
    18. "Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase."
      Larkin C., Datta S., Harley M.J., Anderson B.J., Ebie A., Hargreaves V., Schildbach J.F.
      Structure 13:1533-1544(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 1-330 BOUND TO SS-DNA AND MAGNESIUM, CHARACTERIZATION OF RELAXASE CATALYTIC RESIDUE, MUTAGENESIS OF MET-1; SER-3; TYR-16; LYS-88; ARG-237 AND ILE-241.
      Plasmid: F
    19. "Disrupting antibiotic resistance propagation by inhibiting the conjugative DNA relaxase."
      Lujan S.A., Guogas L.M., Ragonese H., Matson S.W., Redinbo M.R.
      Proc. Natl. Acad. Sci. U.S.A. 104:12282-12287(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-300 IN COMPLEX WITH SS-DNA WITH AND WITHOUT INHIBITOR, ENZYME REGULATION, MUTAGENESIS OF HIS-159.
      Plasmid: F
    20. "A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer."
      Guogas L.M., Kennedy S.A., Lee J.H., Redinbo M.R.
      J. Mol. Biol. 386:554-568(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1476-1628, DNA-BINDING BY C-TERMINUS, MUTAGENESIS OF 1517-ALA--GLY-1525; 1574-LEU-GLN-1575; VAL-1603 AND 1721-GLU--ASP-1756, DISRUPTION PHENOTYPE.
      Plasmid: F

    Entry informationi

    Entry nameiTRAI1_ECOLI
    AccessioniPrimary (citable) accession number: P14565
    Secondary accession number(s): Q51811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme, Plasmid

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3