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yobH yobH recF recF recA recA lexA lexA yneA yneA yoaM yoaM rtbI rtbI yoqW yoqW uvrX uvrX polYB polYB polYA polYA recN recN ruvB ruvB ruvA ruvA uvrC uvrC uvrA uvrA uvrB uvrB yozK yozK yobE yobE
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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yobHPutative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the DNA polymerase type-Y family. (217 aa)
recFDNA repair and genetic recombination factor; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. Is recruited to repair centers, foci that are the site of double- strand DNA break(s) after RecN and RecO; recruitment may depend on RecO. (370 aa)
recAMultifunctional SOS repair factor; Multifunctional protein involved in homologous recombination, DNA repair and competence. Can catalyze the hydrolysis of (d)ATP in the presence of single-stranded DNA; prefers dATP at least in vitro, catalyzes the dATP-dependent uptake of single- stranded DNA by duplex DNA, and the dATP-dependent hybridization of homologous single-stranded DNAs (strand exchange). RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. It interacts with LexA causing its activation and leading to its autocatalytic clea [...] (348 aa)
lexATranscriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. (205 aa)
yneACell division inhibitor; Inhibits cell division during the SOS response. Affects a later stage of the cell division protein assembly, after the assembly of the Z ring, by probably suppressing recruitment of FtsL and/or DivIC to the division machinery (By similarity). (105 aa)
yoaMConserved hypothetical protein; Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross- link with DNA (By similarity). May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). (227 aa)
rtbIRibonuclease toxin of toxin-antitoxin systems RttI-RttJ; Probable DNA helicase. Required for DNA repair and intramolecular recombination; probably has overlapping function with RecS (AC P50729). It probably acts to help generate ss-DNA from ds-DNA breaks; Belongs to the helicase family. RecQ subfamily. (591 aa)
yoqWConserved hypothetical protein; Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross- link with DNA (By similarity). May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). (224 aa)
uvrXLesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. (416 aa)
polYBY family DNA polymerase V bypassing lesions during replication; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity). (412 aa)
polYADNA-damage lesion bypass DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity). (414 aa)
recNFactor for double strand breaks DNA repair and genetic recombination; Involved in recombinational repair of damaged DNA. Seems to be the first protein recruited to repair centers, foci that are the site of double-strand DNA break(s), followed by RecO and then RecF. (576 aa)
ruvBHolliday junction DNA helicase, ATP-dependent component; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing (By similarity). Stimulates the resolution of Holliday junctions by RecU. (334 aa)
ruvAHolliday junction DNA helicase; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (201 aa)
uvrCExcinuclease ABC (subunit C); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. (590 aa)
uvrAExcinuclease ABC (subunit A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. (957 aa)
uvrBExcinuclease ABC (subunit B); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociat [...] (661 aa)
yozKPutative DNA repair protein fragment; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; extrachromosomal origin. (115 aa)
yobEPutative phage protein; Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross- link with DNA (By similarity). May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). (219 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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