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P14565

- TRAI1_ECOLI

UniProt

P14565 - TRAI1_ECOLI

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Protein

Multifunctional conjugation protein TraI

Gene
traI, ECOK12F104
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.5 Publications
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.5 Publications

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 activity Inferred
Active sitei17 – 171Relaxase Reviewed prediction
Metal bindingi146 – 1461Magnesium; via pros nitrogen; catalytic
Metal bindingi157 – 1571Magnesium; via tele nitrogen; catalytic
Metal bindingi159 – 1591Magnesium; via tele nitrogen; catalytic

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi992 – 9998ATP Reviewed prediction

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 Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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.
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.3 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.

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 – 175337 Reviewed predictionAdd
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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 954954Missing in isoform traI*. VSP_018971Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 746MQDGSN → CRMAVT in AAA83930. 1 Publication

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

« 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: September 3, 2014
This is version 111 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

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