ID B1VVM4_STRGG Unreviewed; 553 AA. AC B1VVM4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 04-NOV-2026, entry version 83. 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=SGR_1379 {ECO:0000313|EMBL:BAG18208.1}; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC OS 13350 / KCC S-0626 / ISP 5235). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18208.1, ECO:0000313|Proteomes:UP000001685}; RN [1] {ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235 RC {ECO:0000313|Proteomes:UP000001685}; RX PubMed=18375553; DOI=10.1128/jb.00204-08; RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., RA Yamashita A., Hattori M., Horinouchi S.; RT "Genome sequence of the streptomycin-producing microorganism Streptomyces RT griseus IFO 13350."; RL J. Bacteriol. 190:4050-4060(2008). RN [2] {ECO:0000313|EMBL:BAG18208.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235 RC {ECO:0000313|Proteomes:UP000001685}; RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., RA Yamashita A., Hattori M., Horinouchi S.; RT "The genome sequence of the streptomycin-producing microorganism RT Streptomyces griseus IFO 13350."; RL J. Bacteriol. 0:0-0(2008). RN [3] {ECO:0000313|EMBL:BAG18208.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235 RC {ECO:0000313|Proteomes:UP000001685}; RX PubMed=18364359; DOI=10.1074/jbc.M710461200; RA Funabashi M., Funa N., Horinouchi S.; RT "Phenolic lipids synthesized by type III polyketide synthase confer RT penicillin resistance on Streptomyces griseus."; RL J. Biol. Chem. 283:13983-13991(2008). RN [4] {ECO:0000313|EMBL:BAG18208.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235 RC {ECO:0000313|Proteomes:UP000001685}; RA Hirano S., Tanaka K., Ohnishi Y., Horinouchi S.; RT "Conditionally positive effect of the TetR-family transcriptional regulator RT AtrA on streptomycin production by Streptomyces griseus."; RL Microbiology 154:905-914(2008). 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; AP009493; BAG18208.1; -; Genomic_DNA. DR RefSeq; WP_012378485.1; NC_010572.1. DR AlphaFoldDB; B1VVM4; -. DR KEGG; sgr:SGR_1379; -. DR PATRIC; fig|455632.4.peg.1390; -. DR eggNOG; COG2203; Bacteria. DR eggNOG; COG2208; Bacteria. DR HOGENOM; CLU_000445_43_3_11; -. DR OMA; AGIHSYM; -. DR Proteomes; UP000001685; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd16936; HATPase_RsbW-like; 1. DR FunFam; 3.30.450.40:FF:000035; PAS sensor protein; 1. DR FunFam; 3.30.565.10:FF:000028; PAS sensor protein; 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; 3.60.40.10; 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; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. 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; PF07228; SpoIIE; 1. DR SMART; SM00065; GAF; 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. 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:UP000001685}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 4..192 FT /note="GAF" FT /evidence="ECO:0000259|SMART:SM00065" FT DOMAIN 213..419 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|SMART:SM00331" SQ SEQUENCE 553 AA; 58860 MW; 6E6337F04E63DC3F CRC64; MVHDHLAWLN EASSRIGTTL DLERTAQELV EFTVPRLADG AAIDLLESVL RGEEGAPADT TQPTVTRAIA VAVIDALANL EPDPVGEIST YEERAVDRCL TQREPVLMAR MGAEDYIRVA ATPRAAALLR EAGVHSYLAV PLVSRGVLLG AADFIRSGTT PPFTDTDLAL AMQLASRAAV FLDNARLYGQ ERERLVALQR SMLPRAMPST PGLDVTAHYA PPTETSGVGG DWYDVVALPG GRSALIVGDV MNHGLSAAAT MGRLRTVART LMALDIAPEH TLARMDLAAR DLDDDQVATC LCAVYDPATR EYTLASAGHP PPLLVDAAGR AAYVDVPPGA PLGSGVIPYT SVRLAAPAGS RLVLCTDGLF KNRNDDVDTQ LEKLRDTVSR MDCAELGTLV ASGTGPGTRF DEAVLLMATS RPVSGAADIV VWELPPDAGA ASVARRLVRE QLDRWNLGGL VDTTELVVSE LVGNALRYGG GPGQLRLLRH DRVTVEVTDT GADLPHIQPP TLSDEGGRGL QLINMLCRRW GSCRTPTGKL VWAEQDITVS ATD //