ID A1T128_MYCVP Unreviewed; 517 AA. AC A1T128; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Mvan_0027 {ECO:0000313|EMBL:ABM10878.1}; OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM10878.1, ECO:0000313|Proteomes:UP000009159}; RN [1] {ECO:0000313|EMBL:ABM10878.1, ECO:0000313|Proteomes:UP000009159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / RC PYR-1 {ECO:0000313|Proteomes:UP000009159}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I.J., Miller C., Richardson P.; RT "Complete sequence of Mycobacterium vanbaalenii PYR-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000511; ABM10878.1; -; Genomic_DNA. DR RefSeq; WP_011777352.1; NC_008726.1. DR AlphaFoldDB; A1T128; -. DR STRING; 350058.Mvan_0027; -. DR KEGG; mva:Mvan_0027; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_025431_0_0_11; -. DR Proteomes; UP000009159; Chromosome. DR GO; GO:0016020; C:membrane; 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 PRINTS; PR01217; PRICHEXTENSN. 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 Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000009159}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 298..316 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 6..235 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT REGION 248..294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 420..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 420..446 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..511 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 517 AA; 53923 MW; B4C383BFAA0C5088 CRC64; MTLVLRYAAR SDRGLVRANN EDSVYAGARL LALADGMGGH AAGEVASQLV IAALAHLDDD EPGGDLLSKL DSAVREGNSA IAAHVEADPE LDGMGTTLTA ILFAGNRLGL VHIGDSRGYL LRDGELTQIT KDDTFVQTLV DEGRITAEEA HSHPQRSLIM RALTGHEVEP TLIMREARAG DRYLLCSDGL SDPVSHDTIA EALQIEDVAE SADRLIELAL RGGGPDNVTV VVADVVDYDY GQTQPILAGA VSGDDDQSDP PNTAAGRASA FNPKRNAAKR VVPQPEEPPP RPHSRRRMII AAAVLVLVVL TGLAVGREIV RNNYYVSEHN GTVSIMRGVQ GSFLGVSLQE PYLLGCLNAR NELSLISAGQ SQDSLDCRLL GVGDMRPSER AQVIAGLPSG SLDEAIGQIE ELARSSVLPV CAPPAPPSTT RPPAPSPRPA PAPTSTAPQT TGPSTTPRAS GPAPAPETPR TVTTTAPSPA SPAPVPPASP TPPPPPPTVT ALPPPPPEPG TNCREVS //