ID Q2JBH9_FRACC Unreviewed; 722 AA. AC Q2JBH9; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 109. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; DE AltName: Full=Protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00081350}; DE AltName: Full=Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00075117}; GN OrderedLocusNames=Francci3_1989 {ECO:0000313|EMBL:ABD11363.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales; OC Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD11363.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD11363.1, ECO:0000313|Proteomes:UP000001937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45818 / CECT 9043 / CcI3 RC {ECO:0000313|Proteomes:UP000001937}; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C., RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., RA Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: Primarily acts as an independent SigF regulator that is CC sensitive to the osmosensory signal, mediating the cross talk of PknD CC with the SigF regulon. Possesses both phosphatase and kinase CC activities. The kinase domain functions as a classic anti-sigma factor- CC like kinase to phosphorylate the anti-anti-sigma factor domain at the CC canonical regulatory site, and the phosphatase domain antagonizes this CC activity. {ECO:0000256|ARBA:ARBA00056274}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00047761}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000249; ABD11363.1; -; Genomic_DNA. DR AlphaFoldDB; Q2JBH9; -. DR STRING; 106370.Francci3_1989; -. DR KEGG; fra:Francci3_1989; -. DR eggNOG; COG2208; Bacteria. DR HOGENOM; CLU_000445_43_3_11; -. DR OrthoDB; 118142at2; -. DR PhylomeDB; Q2JBH9; -. DR Proteomes; UP000001937; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd16936; HATPase_RsbW-like; 1. DR CDD; cd00130; PAS; 1. DR FunFam; 3.60.40.10:FF:000005; Serine/threonine protein phosphatase; 1. DR Gene3D; 3.30.450.40; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR052016; Bact_Sigma-Reg. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF-like_dom_sf. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. DR InterPro; IPR000014; PAS. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013656; PAS_4. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR43156:SF2; STAGE II SPORULATION PROTEIN E; 1. DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1. DR Pfam; PF01590; GAF; 1. DR Pfam; PF13581; HATPase_c_2; 1. DR Pfam; PF08448; PAS_4; 1. DR Pfam; PF07228; SpoIIE; 1. DR SMART; SM00065; GAF; 1. DR SMART; SM00091; PAS; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF55781; GAF domain-like; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}; KW Reference proteome {ECO:0000313|Proteomes:UP000001937}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 29..92 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" SQ SEQUENCE 722 AA; 78284 MW; 35BCBBA31E084B5F CRC64; MTSEPRRTLS DVSSDYALDA GFDSLLGTQL IDFSPTAMVI IDPDLRVRRS NRSFREIYGL SPEQLAGTSI PELLPDMDPR VWKLARWVLA SGESVEDTEI IGRSVAFPQE ERTWRFSHFP LRDREGVPAA VGVTLVDVTD QRRAERKHAE AERRLRLLTR ASTLVGRSLE LDATLASIAD FMVPEFADTC SVYLLDEPLD TDARPELLEL RRAIKTRVSG PPLQSCDIPF SAAGEILYCH RNSPIYQAFA SGRPFHHAAD DESLISGYQT PGFLDYFRRL LLRWGIAVPL LVGRYFHGVM VVHVGVSGRT YTDDDVEMAA NLGGRISAAI ANARAYARER EVSVTLQRSL LAPDIPAVAG MDIAWRYEPG SLPGRSPCAE PGPPIDAEVG GDWFDLIPLS AGRVALVIGD VAGRGVTAAA VMGQLRTASR AFASLDLPAD DVLTHLDNLA QTIGAGPDGA LASCVYAIFE PTTATIVLAN AGHPPPALRD PDGRVRLLTG GGGAFLGIGG QVFVQTCYPF PVGATLALYT DGLVESRDID IFQGIGRLQH ALADAGTADA TADRLMRLVD QANRDDDVAL LLVRAAAAIN TRTLTIPLTL DLRAVGQARH AVNAALRRWQ QPETIETAEL LVSEIVTNAI RYSRVPGELV LRSVPTALYI EVSDSDSHLP RVLHPNEQEE HGRGLILVDA LAARWGTRPT HSGKTVWCQL DTGTDTGPEI FT //