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Consequently, we sought to identify a Ser\/Thr protein phosphatase partner for the chlamydial kinases. CTL0511 from\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Chlamydia trachomatis<\/jats:named-content>\n            L2 434\/Bu, which has homologs in all sequenced\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Chlamydia<\/jats:named-content>\n            spp., is a predicted type 2C Ser\/Thr protein phosphatase (PP2C). Recombinant maltose-binding protein (MBP)-tagged CTL0511 (rCTL0511) hydrolyzed\n            <jats:italic>p<\/jats:italic>\n            -nitrophenyl phosphate (pNPP), a generic phosphatase substrate, in a MnCl\n            <jats:sub>2<\/jats:sub>\n            -dependent manner at physiological pH. Assays using phosphopeptide substrates revealed that rCTL0511 can dephosphorylate phosphorylated serine (P-Ser), P-Thr, and P-Tyr residues using either MnCl\n            <jats:sub>2<\/jats:sub>\n            or MgCl\n            <jats:sub>2<\/jats:sub>\n            , indicating that metal usage can alter substrate preference. Phosphatase activity was unaffected by PP1, PP2A, and PP3 phosphatase inhibitors, while mutation of conserved PP2C residues significantly inhibited activity. Finally, phosphatase activity was detected in elementary body (EB) and reticulate body (RB) lysates, supporting a role for protein dephosphorylation in chlamydial development. These findings support that CTL0511 is a metal-dependent protein phosphatase with broad substrate specificity, substantiating a reversible phosphorylation network in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">C. trachomatis<\/jats:named-content>\n            .\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Chlamydia<\/jats:named-content>\n            spp. are obligate intracellular bacterial pathogens responsible for a variety of diseases in humans and economically important animal species. Our work demonstrates that\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Chlamydia<\/jats:named-content>\n            spp. produce a PP2C capable of dephosphorylating P-Thr, P-Ser, and P-Tyr and that\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Chlamydia trachomatis<\/jats:named-content>\n            EBs and RBs possess phosphatase activity. In conjunction with the chlamydial Hanks'-type kinases Pkn1 and PknD, validation of CTL0511 fulfills the enzymatic requirements for a reversible phosphoprotein network. As protein phosphorylation regulates important cellular processes, including metabolism, differentiation, and virulence, in other bacterial pathogens, these results set the stage for elucidating the role of global protein phosphorylation in chlamydial physiology and virulence.\n          <\/jats:p>","DOI":"10.1128\/jb.00025-16","type":"journal-article","created":{"date-parts":[[2016,4,26]],"date-time":"2016-04-26T03:49:46Z","timestamp":1461642586000},"page":"1827-1836","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":7,"title":["CTL0511 from Chlamydia trachomatis Is a Type 2C Protein Phosphatase with Broad Substrate Specificity"],"prefix":"10.1128","volume":"198","author":[{"given":"Ja E.","family":"Claywell","sequence":"first","affiliation":[{"name":"Department of Microbiology, Southern Illinois University, Carbondale, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Derek J.","family":"Fisher","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Southern Illinois University, Carbondale, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1086\/652397"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.62.081307.162818"},{"key":"e_1_3_3_4_2","unstructured":"Centers for Disease Control and Prevention. 2014. 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