ID A4XC84_SALTO Unreviewed; 239 AA. AC A4XC84; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Strop_4111 {ECO:0000313|EMBL:ABP56541.1}; OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC OS 105044 / CNB-440). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Salinispora. OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP56541.1, ECO:0000313|Proteomes:UP000000235}; RN [1] {ECO:0000313|Proteomes:UP000000235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440 RC {ECO:0000313|Proteomes:UP000000235}; RX PubMed=17563368; DOI=10.1073/pnas.0700962104; RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W., RA Jensen P.R., Moore B.S.; RT "Genome sequencing reveals complex secondary metabolome in the marine RT actinomycete Salinispora tropica."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = 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:ARBA00001512}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001482}; 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; CP000667; ABP56541.1; -; Genomic_DNA. DR RefSeq; WP_012015309.1; NC_009380.1. DR AlphaFoldDB; A4XC84; -. DR STRING; 369723.Strop_4111; -. DR KEGG; stp:Strop_4111; -. DR PATRIC; fig|369723.5.peg.4251; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_0_2_11; -. DR Proteomes; UP000000235; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000000235}. FT DOMAIN 6..236 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 239 AA; 24899 MW; C3EBBFE61010B67C CRC64; MTLILRSAIR NDIGLVRNNN EDSALAGERL LAVADGMGGL PAGEVASEIV IRILDELTPP STPAEAADAL RAVVSAANQR IHAAIAADPA REGMGTTLTA ALLADDTLVL AQVGDSRCYL LRDGELTLIT RDDTFVQALV DQGAITPEQA RHHPQRSLVT RAVQGAGAPP AIGILTVASG DRLLLCSDGL SDYVEHEAIT ATLTQHGDRQ LCGEQLVKLA HQAGAPDNVT VVVSDVITA //