Plasmid F traI:Gene Product(s)
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Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
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Standard name |
traI |
---|---|
Synonyms |
traI, Fpla107 |
Product description |
traI required for DNA transfer; nicks the DNA at oriT through N-terminal domain; C-terminal domain is a helicase that unwinds the DNA |
EC number (for enzymes) |
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Notes
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0003678 |
DNA helicase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
GO:0003697 |
single-stranded DNA binding |
IDA: Inferred from Direct Assay |
F |
See Figure 1. |
complete | |||
GO:0004003 |
ATP-dependent DNA helicase activity |
IDA: Inferred from Direct Assay |
F |
See Table III |
complete | |||
GO:0043141 |
ATP-dependent 5'-3' DNA helicase activity |
IDA: Inferred from Direct Assay |
F |
See Fig. 3 |
complete | |||
GO:0017116 |
single-stranded DNA-dependent ATP-dependent DNA helicase activity |
IDA: Inferred from Direct Assay |
F |
See Table 1 and Table 2. |
complete | |||
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Interactions <protect> See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
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Notes
Localization
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Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
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Sequence |
MMSIAQVRSA GSAGNYYTDK DNYYVLGSMG ERWAGRGAEQ LGLQGSVDKD VFTRLLEGRL PDGADLSRMQ DGSNRHRPGY DLTFSAPKSV SMMAMLGGDK RLIDAHNQAV DFAVRQVEAL ASTRVMTDGQ SETVLTGNLV MALFNHDTSR DQEPQLHTHA VVANVTQHNG EWKTLSSDKV GKTGFIENVY ANQIAFGRLY REKLKEQVEA LGYETEVVGK HGMWEMPGVP VEAFSGRSQT IREAVGEDAS LKSRDVAALD TRKSKQHVDP EIKMAEWMQT LKETGFDIRA YRDAADQRAD LRTLTPGPAS QDGPDVQQAV TQAIAGLSER KVQFTYTDVL ARTVGILPPE NGVIERARAG IDEAISREQL IPLDREKGLF TSGIHVLDEL SVRALSRDIM KQNRVTVHPE KSVPRTAGYS DAVSVLAQDR PSLAIVSGQG GAAGQRERVA ELVMMAREQG REVQIIAADR RSQMNMKQDE RLSGELITGR RQLLEGMAFT PGSTVIVDQG EKLSLKETLT LLDGAARHNV QVLITDSGQR TGTGSALMAM KDAGVNTYRW QGGEQRPATI ISEPDRNVRY ARLAGDFAAS VKAGEESVAQ VSGVREQAIL TQAIRSELKT QGVLGLPEVT MTALSPVWLD SRSRYLRDMY RPGMVMEQWN PETRSHDRYV IDRVTAQSHS LTLRDAQGET QVVRISSLDS SWSLFRPEKM PVADGERLRV TGKIPGLRVS GGDRLQVASV SEDAMTVVVP GRAEPATLPV SDSPFTALKL ENGWVETPGH SVSDSATVFA SVTQMAMDNA TLNGLARSGR DVRLYSSLDE TRTAEKLARH PSFTVVSEQI KTRAGETSLE TAISHQKSAL HTPAQQAIHL ALPVVESKKL AFSMVDLLTE AKSFAAEGTG FTELGGEINA QIKRGDLLYV DVAKGYGTGL LVSRASYEAE KSILRHILEG KEAVMPLMER VPGELMEKLT SGQRAATRMI LETSDRFTVV QGYAGVGKTT QFRAVMSAVN MLPESERPRV VGLGPTHRAV GEMRSAGVDA QTLASFLHDT QLQQRSGETP DFSNTLFLLD ESSMVGNTDM ARAYALIAAG GGRAVASGDT DQLQAIAPGQ PFRLQQTRSA ADVAIMKEIV RQTPELREAV YSLINRDVER ALSGLESVKP SQVPRQEGAW APEHSVTEFS HSQEAKLAEA QQKAMLKGEA FPDVPMTLYE AIVRDYTGRT PEAREQTLIV THLNEDRRVL NSMIHDVREK AGELGKEQVM VPVLNTANIR DGELRRLSTW ETHRDALVLV DNVYHRIAGI SKDDGLITLQ DAEGNTRLIS PREAVAEGVT LYTPDTIRVG TGDRMRFTKS DRERGYVANS VWTVTAVSGD SVTLSDGQQT REIRPGQEQA EQHIDLAYAI TAHGAQGASE TFAIALEGTE GNRKLMAGFE SAYVALSRMK QHVQVYTDNR QGWTDAINNA VQKGTAHDVF EPKPDREVMN AERLFSTARE LRDVAAGRAV LRQAGLAGGD SPARFIAPGR KYPQPYVALP AFDRNGKSAG IWLNPLTTDD GNGLRGFSGE GRVKGSGDAQ FVALQGSRNG ESLLADNMQD GVRIARDNPD SGVVVRIAGE GRPWNPGAIT GGRVWGDIPD NSVQPGAGNG EPVTAEVLAQ RQAEEAIRRE TERRADEIVR KMAENKPDLP DGKTEQAVRE IAGQERDRAA ITEREAALPE GVLREPQRVR EAVREIAREN LLQERLQQME RDMVRDLQKE KTLGGD |
Length |
1,756 |
Mol. Wt |
192.014 kDa |
pI |
6.0 (calculated) |
Extinction coefficient |
137,170 (calc based on 33 Y, 16 W, and 0 C residues) |
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Domains/Motifs/Modification Sites
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
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Resource type | Source | Notes/Reference |
---|---|---|
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
EcoCyc: |
Escherichia coli str. K-12 substr. MG1655 | |
EcoGene: |
Escherichia coli str. K-12 substr. MG1655 | |
RegulonDB: |
Escherichia coli str. K-12 substr. MG1655 | |
EchoBASE: |
Escherichia coli str. K-12 substr. MG1655 | |
ASAP: |
Escherichia coli str. K-12 substr. MG1655 | |
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Notes
Links
Name | URL | Comments |
---|---|---|
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References
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- ↑ Reygers, U et al. (1991) Endonuclease activity of Escherichia coli DNA helicase I directed against the transfer origin of the F factor. EMBO J. 10 2689-94 PubMed
- ↑ Hekman, K et al. (2008) An intrastrand three-DNA-base interaction is a key specificity determinant of F transfer initiation and of F TraI relaxase DNA recognition and cleavage. Nucleic Acids Res. 36 4565-72 PubMed
- ↑ 3.0 3.1 Lahue, EE & Matson, SW (1988) Escherichia coli DNA helicase I catalyzes a unidirectional and highly processive unwinding reaction. J. Biol. Chem. 263 3208-15 PubMed
- ↑ Abdel-Monem, M et al. (1977) Enzymatic unwinding of DNA. III. Mode of action of Escherichia coli DNA unwinding enzyme. J. Mol. Biol. 110 667-85 PubMed
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