DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family.

DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4.

DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family.

Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187.

DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4.

DNA methylase M, host modification; Methylation of specific adenine residues; required for both restriction and modification activities (By similarity). The StySJI enzyme recognizes 5'-GAGN(6)GTRC-3'; Belongs to the N(4)/N(6)-methyltransferase family.

DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

DNA methylase; Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4.

Putative Smr domain protein; Similar to E. coli orf, hypothetical protein (AAC74422.1); Blastp hit to AAC74422.1 (187 aa), 86% identity in aa 1 - 187.

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy.

Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.

Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.

Similar to E. coli RNase I, cleaves phosphodiester bond between any two nucleotides (AAC73712.1); Blastp hit to AAC73712.1 (268 aa), 73% identity in aa 1 - 268; Belongs to the RNase T2 family.

Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy.

Similar to E. coli RNase I, cleaves phosphodiester bond between any two nucleotides (AAC73712.1); Blastp hit to AAC73712.1 (268 aa), 73% identity in aa 1 - 268; Belongs to the RNase T2 family.

Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy.

Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...]

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy.

DNA strand exchange and recombination protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.