InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures

PAO1, PA5443 (uvrD) Cytoplasmic. Cytoplasmic Membrane. Periplasmic. Outer Membrane. Extracellular. Unknown. View in JBrowse View in GBrowse PseudoCyc / Metabolic Pathways. Overview.

C. Hodgman, Nature 333:22–23, 1988) associated with the superfamily of proteins of which it is a member. Abstract. Escherichia coli UvrD is a superfamily 1 helicase/translocase that functions in DNA repair, replication, and recombination. Although a UvrD monomer can translocate along single-stranded DNA, self-assembly or interaction with an accessory protein is needed to activate its helicase activity in vitro. Escherichia coli UvrD is a superfamily 1 DNA helicase and single-stranded DNA (ssDNA) translocase that functions in DNA repair and plasmid replication and as an anti-recombinase by removing RecA protein from ssDNA. UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality. 2009-02-23 · Expansion occurred at an increased rate in cells lacking dam, polA, rnhA, or uvrD functions.

Uvrd function

Additional regulatory proteins may remain to be discovered. 2020-10-23 · This feature of UvrD-CTD points to an essential function as a protein-ligand binding hub facilitating the RNAP interaction. UvrD-CTD Tudor domain interacts with DNA non-specifically. UvrD (DNA helicase II) is a prototypical superfamily 1 (SF 1) helicase involved primarily in nucleotide excision repair and methyl-directed mismatch repair in Escherichia coli (1, 2). uvrD in E. coli remains viable, although it is lethal in either a polA or rep background, and exhibits sensiti-vity to UV light, elevated rates of recombination and mutations [17].

Therefore, the function of UvrD that allows RFR at dnaNts ‐blocked forks in the presence of RecQJFORA is inactivated by the uvrD252 mutation, suggesting a requirement for the helicase or the translocase function of UvrD to counteract RecQJFORA in this replication mutant. The RFR defect of the uvrD mutant is suppressed by Bacillus subtilis PcrA

In conclusion, our results show that UvrD has multiple functions at inactivated replication forks, which are all linked to the action of recombination proteins but by different means. We previously reported that to remove DNA‐bound Tus protein, UvrD acts in concert with RecBCD‐dependent homologous recombination (Bidnenko et al, 2006).

Escherichia coli UvrD is a 3′–5′ superfamily 1A helicase/translocase involved in a variety of DNA metabolic processes. UvrD can function either as a helicase or only as an single‐stranded DNA (ssDNA) translocase. The switch between these activities is controlled in vitro by the UvrD oligomeric state; a monomer has ssDNA translocase activity, whereas at least a dimer is needed for

2020 — UvrD helicase-RNA polymerase interactions are governed by UvrD's Function, and Can Transdifferentiate into Brown-like Adipocytes. He investigates macromolecular protein machines by high-resolution Nuclear Magnetic Resonance (NMR) underlying essential cellular functions. Group home (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) GN=uvrD PE=4 function in citronellol catabolism OS=Pseudomonas aeruginosa (strain ATCC UvrD/REP helicase OS=Chloroflexus aurantiacus (strain ATCC 29366 / DSM >tr|A9WAY8|A9WAY8_CHLAA Cell envelope-related function transcriptional 116, CLS10264, n, Y, n, Y, Y, Y, n, 1, 1, 1, 1, 2, 0, 0, 0, 0, 0, UvrD/REP helicase family protein 0, 0, protein of unknown function DUF305 conserved in bacteria. match hypothetical coding sequences of unknown function and the remaining 448 scoB murE mraY1 murF 524 sppA uvrD 678 681 tmk 679 682 proP4 ubiE Amplification and Magnetics) functions by capturing single DNA molecules on Characterization of a thermostable UvrD helicase and its participation in Below, we review the functions of UvrD, Rep and PcrA and their potential roles in shown that UvrD can remove RecA filaments from DNA, and this function has Frekvenser med mera matas in med hjälp av datastav R-168 UVRD-O. Kryptering av kommunikation kan ske via en inbyggd funktion, men externa och mer carrying an UvrD-like helicase C-terminal domain, and two contiguous putative serine/threonine protein kinases (Fig. 6). The specific role of these mutations in 44 (mutH, mutL, mutS, uvrD) indikerar en mutatorspänning.

1 Publication 2012-05-09 We find that H. pylori UvrD functions to repair DNA damage and limit homologous recombination and DNA damage-induced genomic rearrangements between DNA repeats. Our results suggest that UvrD and other NER pathway proteins play a prominent role in maintaining genome integrity, especially after DNA damage; thus, NER may be especially critical in organisms such as H. pylori that face high-level … Therefore, the function of UvrD that allows RFR at dnaNts ‐blocked forks in the presence of RecQJFORA is inactivated by the uvrD252 mutation, suggesting a requirement for the helicase or the translocase function of UvrD to counteract RecQJFORA in this replication mutant. The RFR defect of the uvrD mutant is suppressed by Bacillus subtilis PcrA UvrD, a helicase with multiple functions in vivo, one of which is to remove RecA from ssDNA (Veaute et al.
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Here we present measurements of UvrD, a DNA repair 2018-10-19 2009-04-03 uvrD homolog has been shown to partially compensate for the repair function of E. coli UvrD, suggesting that the function of the helicase is evolutionarily conserved (11). Characterization of this protein indicates that the T. thermophilus UvrD pos-sesses a 3-5 DNA helicase activity similar to the E. coli UvrD (12). Nucleic Acids Research, 2017 1 doi: 10.1093/nar/gkx074 The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase Kelly Sanders1,†, Chia-Liang Lin2,†, Abigail J. Smith1,†, Nora Cronin2, Gemma Fisher1, Vasileios Eftychidis3, Peter McGlynn3, Nigel J. Savery1, Dale B. Wigley2 and Mark S. Dillingham1,* 1DNA:Protein Interactions Unit, School of Biochemistry Tte UvrD Helicase is a repair helicase capable of unwinding double-stranded DNA, without a requirement for a specific flap or overhang structure, from the thermophilic organism Thermoanaerobacter tengcongensis.It is active on a wide range of DNA substrates and, along with its thermostability (active to 70°C), Tte UvrD Helicase has been demonstrated to be a useful additive for improving This video provides two examples of how to determine function values using function notation on the TI84 graphing calculator.

It is required for replication of several rolling-circle plasmids [ 22 ] and copurifies with DNA polymerase III holoenzyme under some conditions [ 23 ]. RecJ functions in both the RecQ and RecA-dependent TLD pathways in UvrD + cells Whereas, RecA, RecF, RecQ, and RecJ act in one linear pathway of hyper-TLD in Δ uvrD cells ( Figures 3B and Figure 4, A, C, and D ), RecQ and RecJ were shown previously to act in one pathway of TLD in UvrD + cells while RecA and RecF acted in a second SOS-response-dependent pathway that is independent of RecQ ( Fonville et al.
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The enzymatic function of UvrD is to translocate along a DNA strand in a 3′ to 5′ direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity. In addition, UvrD interacts with many other proteins involved in the above processes and is hypothesized to facilitate protein turnover, thus promoting further DNA processing.

… 2020-10-23 The enzymatic function of UvrD is to translocate along a DNA strand in a 3' to 5' direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity. In addition, UvrD interacts with many other proteins involved in the above processes and is hypothesized to facilitate protein turnover, thus promoting further DNA processing. 2011-09-01 2015-04-17 2014-01-08 2017-02-04 In addition, UvrD plays critical roles in rolling circle plasmid replication, processing of Okazaki fragments in the absence of DNA polymerase I and replication fork reversal in Escherichia coli polymerase III mutants with multiple functions at inactivated replication forks [[8-11]].

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2020-10-23 · This feature of UvrD-CTD points to an essential function as a protein-ligand binding hub facilitating the RNAP interaction. UvrD-CTD Tudor domain interacts with DNA non-specifically.

All of these proteins function in a network that determines where and how RecA functions.

This video provides two examples of how to determine function values using function notation on the TI84 graphing calculator. The results are verified graph

För var UvrD-like DNA helicase, C-terminal 279 618 1.4E-75 CDD cd18807 SF1_C_UvrD 287 616 5.00011E-31 ProSiteProfiles PS51198 UvrD-like DNA helicase ATP-binding domain profile. IPR014016: UvrD-like helicase, ATP-binding domain 10 288 UvrD is an abundant helicase in Escherichia coli with well characterized functions in mismatch and nucleotide excision repair and a possible role in displacement of proteins such as RecA from single-stranded DNA. The mismatch repair protein MutL is known to stimulate UvrD. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA (PubMed: 8419285 ). Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable).1 Publication.

The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. 2009-04-03 · Whether this protein displacement function requires specific recruitment of UvrD or merely reflects the abundance of UvrD in vivo remains unknown. Facilitation by UvrAB of nicked duplex unwinding by UvrD provides an explanation as to why UvrA, -B, and -D are all required to maintain viability in the absence of DNA polymerase I ( 51 ). measurements simultaneously. Here we present measurements of UvrD, a DNA repair helicase, that directly and unambiguously reveal the connection between its structure and function.