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P14565

- TRAI1_ECOLI

UniProt

P14565 - TRAI1_ECOLI

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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

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MMSIAQVRSA GSAGNYYTDK DNYYVLGSMG ERWAGRGAEQ LGLQGSVDKD
60 70 80 90 100
VFTRLLEGRL PDGADLSRMQ DGSNRHRPGY DLTFSAPKSV SMMAMLGGDK
110 120 130 140 150
RLIDAHNQAV DFAVRQVEAL ASTRVMTDGQ SETVLTGNLV MALFNHDTSR
160 170 180 190 200
DQEPQLHTHA VVANVTQHNG EWKTLSSDKV GKTGFIENVY ANQIAFGRLY
210 220 230 240 250
REKLKEQVEA LGYETEVVGK HGMWEMPGVP VEAFSGRSQT IREAVGEDAS
260 270 280 290 300
LKSRDVAALD TRKSKQHVDP EIKMAEWMQT LKETGFDIRA YRDAADQRAD
310 320 330 340 350
LRTLTPGPAS QDGPDVQQAV TQAIAGLSER KVQFTYTDVL ARTVGILPPE
360 370 380 390 400
NGVIERARAG IDEAISREQL IPLDREKGLF TSGIHVLDEL SVRALSRDIM
410 420 430 440 450
KQNRVTVHPE KSVPRTAGYS DAVSVLAQDR PSLAIVSGQG GAAGQRERVA
460 470 480 490 500
ELVMMAREQG REVQIIAADR RSQMNMKQDE RLSGELITGR RQLLEGMAFT
510 520 530 540 550
PGSTVIVDQG EKLSLKETLT LLDGAARHNV QVLITDSGQR TGTGSALMAM
560 570 580 590 600
KDAGVNTYRW QGGEQRPATI ISEPDRNVRY ARLAGDFAAS VKAGEESVAQ
610 620 630 640 650
VSGVREQAIL TQAIRSELKT QGVLGLPEVT MTALSPVWLD SRSRYLRDMY
660 670 680 690 700
RPGMVMEQWN PETRSHDRYV IDRVTAQSHS LTLRDAQGET QVVRISSLDS
710 720 730 740 750
SWSLFRPEKM PVADGERLRV TGKIPGLRVS GGDRLQVASV SEDAMTVVVP
760 770 780 790 800
GRAEPATLPV SDSPFTALKL ENGWVETPGH SVSDSATVFA SVTQMAMDNA
810 820 830 840 850
TLNGLARSGR DVRLYSSLDE TRTAEKLARH PSFTVVSEQI KTRAGETSLE
860 870 880 890 900
TAISHQKSAL HTPAQQAIHL ALPVVESKKL AFSMVDLLTE AKSFAAEGTG
910 920 930 940 950
FTELGGEINA QIKRGDLLYV DVAKGYGTGL LVSRASYEAE KSILRHILEG
960 970 980 990 1000
KEAVMPLMER VPGELMEKLT SGQRAATRMI LETSDRFTVV QGYAGVGKTT
1010 1020 1030 1040 1050
QFRAVMSAVN MLPESERPRV VGLGPTHRAV GEMRSAGVDA QTLASFLHDT
1060 1070 1080 1090 1100
QLQQRSGETP DFSNTLFLLD ESSMVGNTDM ARAYALIAAG GGRAVASGDT
1110 1120 1130 1140 1150
DQLQAIAPGQ PFRLQQTRSA ADVAIMKEIV RQTPELREAV YSLINRDVER
1160 1170 1180 1190 1200
ALSGLESVKP SQVPRQEGAW APEHSVTEFS HSQEAKLAEA QQKAMLKGEA
1210 1220 1230 1240 1250
FPDVPMTLYE AIVRDYTGRT PEAREQTLIV THLNEDRRVL NSMIHDVREK
1260 1270 1280 1290 1300
AGELGKEQVM VPVLNTANIR DGELRRLSTW ETHRDALVLV DNVYHRIAGI
1310 1320 1330 1340 1350
SKDDGLITLQ DAEGNTRLIS PREAVAEGVT LYTPDTIRVG TGDRMRFTKS
1360 1370 1380 1390 1400
DRERGYVANS VWTVTAVSGD SVTLSDGQQT REIRPGQEQA EQHIDLAYAI
1410 1420 1430 1440 1450
TAHGAQGASE TFAIALEGTE GNRKLMAGFE SAYVALSRMK QHVQVYTDNR
1460 1470 1480 1490 1500
QGWTDAINNA VQKGTAHDVF EPKPDREVMN AERLFSTARE LRDVAAGRAV
1510 1520 1530 1540 1550
LRQAGLAGGD SPARFIAPGR KYPQPYVALP AFDRNGKSAG IWLNPLTTDD
1560 1570 1580 1590 1600
GNGLRGFSGE GRVKGSGDAQ FVALQGSRNG ESLLADNMQD GVRIARDNPD
1610 1620 1630 1640 1650
SGVVVRIAGE GRPWNPGAIT GGRVWGDIPD NSVQPGAGNG EPVTAEVLAQ
1660 1670 1680 1690 1700
RQAEEAIRRE TERRADEIVR KMAENKPDLP DGKTEQAVRE IAGQERDRAA
1710 1720 1730 1740 1750
ITEREAALPE GVLREPQRVR EAVREIAREN LLQERLQQME RDMVRDLQKE

KTLGGD
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 114 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