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Fig. S1. Alignment of three putative tyrosine recombinases of Ureaplasma parvum serovar 3 (ATCC 700970 and ATCC 27815T).

Fig. S2. Annealed oligonucleotides for EMSA analyses.

Fig. S3. Plasmid pMT::mbatrunc.

Fig. S4. Promoter fusion and Mrfp1 expression from Ureaplasma promoters in Mycoplasma pneumoniae M129.

Fig. S5. Growth curve of MBP::CodV expressing Escherichia coli.

Fig. S6. Protein expression and purification of MBP fusion proteins.

Fig. S7. Cell morphology of MBP::CodV expressing Escherichia coli.

Fig. S8. Protein preparations for EMSA analyses.

Fig. S9. Protein concentration-dependent binding of MBP::RipX and MBP::XerC to DR20-kb.

Fig. S10. Protein-DNA interaction.

Fig. S11. Inhibition of XerC binding to IRmba by EDTA.

Fig. S12. Integration of mbatrunc into the Mycoplasma pneumoniae chromosome.

Fig. S13. Protein concentration-dependent binding of MBP::RipX and MBP::XerC to IRmba.

Fig. S14. Protein concentration-dependent binding of MBP::XerC to IRmba on a 145-bp PCR product.

Fig. S15. Protein concentration-dependent binding of MBP::CodV and the soluble fraction of Escherichia coli DH10B to difUP.

Table S1. Occurrence of the three putative tyrosine recombinase-encoding genes ripX, xerC and codV in Ureaplasma serovars, the translocase encoding gene ftsK and genes encoding topoisomerase subunits parE and parC.

Table S2. Growth of MBP::CodV expressing Escherichia coli.

Table S3. Features of proteins used for EMSA analyses.

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