ID A0QTQ6_MYCS2 Unreviewed; 233 AA. AC A0QTQ6; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=MSMEG_1928 {ECO:0000313|EMBL:ABK75945.1}; OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium OS smegmatis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75945.1, ECO:0000313|Proteomes:UP000000757}; RN [1] {ECO:0000313|EMBL:ABK75945.1, ECO:0000313|Proteomes:UP000000757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757}; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:2V06} RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH MAGNESIUM. RX PubMed=17961594; DOI=10.1016/j.jmb.2007.09.076; RA Wehenkel A., Bellinzoni M., Schaeffer F., Villarino A., Alzari P.M.; RT "Structural and binding studies of the three-metal center in two RT mycobacterial PPM Ser/Thr protein phosphatases."; RL J. Mol. Biol. 374:890-898(2007). RN [3] {ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFS} RP X-RAY CRYSTALLOGRAPHY (0.83 ANGSTROMS) IN COMPLEX WITH MANGANESE. RX PubMed=17637345; DOI=10.1016/j.str.2007.06.002; RA Bellinzoni M., Wehenkel A., Shepard W., Alzari P.M.; RT "Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the RT atomic resolution structures of a mycobacterial enzyme."; RL Structure 15:863-872(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; CP000480; ABK75945.1; -; Genomic_DNA. DR RefSeq; WP_011728018.1; NZ_SIJM01000020.1. DR RefSeq; YP_886294.1; NC_008596.1. DR PDB; 2JFR; X-ray; 0.83 A; A=1-233. DR PDB; 2JFS; X-ray; 1.45 A; A=1-233. DR PDB; 2JFT; X-ray; 1.08 A; A=1-233. DR PDB; 2V06; X-ray; 1.05 A; A=1-233. DR PDBsum; 2JFR; -. DR PDBsum; 2JFS; -. DR PDBsum; 2JFT; -. DR PDBsum; 2V06; -. DR AlphaFoldDB; A0QTQ6; -. DR SMR; A0QTQ6; -. DR STRING; 246196.MSMEG_1928; -. DR PaxDb; 246196-MSMEI_1887; -. DR GeneID; 66733362; -. DR KEGG; msm:MSMEG_1928; -. DR PATRIC; fig|246196.19.peg.1909; -. DR eggNOG; COG0631; Bacteria. DR OrthoDB; 9801841at2; -. DR EvolutionaryTrace; A0QTQ6; -. DR Proteomes; UP000000757; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFS}; KW Metal-binding {ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFS}; KW Reference proteome {ECO:0000313|Proteomes:UP000000757}. FT DOMAIN 6..232 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT BINDING 35 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFT" FT BINDING 35 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2V06" FT BINDING 35 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JFS" FT BINDING 35 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFS" FT BINDING 36 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFT" FT BINDING 36 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JFS" FT BINDING 111 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFT" FT BINDING 153 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2JFS" FT BINDING 185 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFT" FT BINDING 185 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2V06" FT BINDING 185 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFS" FT BINDING 185 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2JFS" FT BINDING 223 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2V06" FT BINDING 223 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2JFR, ECO:0007829|PDB:2JFS" SQ SEQUENCE 233 AA; 24198 MW; 5BC95EDB6EC9C6C1 CRC64; MASVLSAATA TDQGPVRENN QDACLADGIL YAVADGFGAR GHHASATALK TLSAGFAAAP DRDGLLEAVQ QANLRVFELL GDEPTVSGTT LTAVAVFEPG QGGPLVVNIG DSPLYRIRDG HMEQLTDDHS VAGELVRMGE ITRHEARWHP QRHLLTRALG IGPHIGPDVF GIDCGPGDRL LISSDGLFAA ADEALIVDAA TSPDPQVAVR RLVEVANDAG GSDNTTVVVI DLG //