ID Q8A432_BACTN Unreviewed; 549 AA. AC Q8A432; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=BT_2772 {ECO:0000313|EMBL:AAO77878.1}; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77878.1, ECO:0000313|Proteomes:UP000001414}; RN [1] {ECO:0000313|EMBL:AAO77878.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414}; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., RA Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). RN [2] {ECO:0000313|EMBL:AAO77878.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414}; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of its two RT dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). 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; AE015928; AAO77878.1; -; Genomic_DNA. DR RefSeq; NP_811684.1; NC_004663.1. DR RefSeq; WP_011108468.1; NZ_UYXG01000001.1. DR AlphaFoldDB; Q8A432; -. DR STRING; 226186.BT_2772; -. DR PaxDb; 226186-BT_2772; -. DR EnsemblBacteria; AAO77878; AAO77878; BT_2772. DR GeneID; 60923950; -. DR KEGG; bth:BT_2772; -. DR PATRIC; fig|226186.12.peg.2819; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_495815_0_0_10; -. DR InParanoid; Q8A432; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000001414; 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 NCBIfam; NF033484; Stp1_PP2C_phos; 1. 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 Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001414}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265..287 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 6..250 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 549 AA; 61382 MW; 1748D827BD1E2B06 CRC64; MKEENIYNYC HIAGRTDIGC KRQANEDSMG NFETINGLAA VVCDGMGGHV GGATASRLAV EAIHGFLDGQ YYEDPREAIG EAIDAANKAI LHQAMIQPEL QGMGSTCVLL LVRDSKVYIG HVGDSRVYLI RNRCIKQLTK DHSYVQMLVD MGQLTNEQAE HHPRKNEITN ALGIANMKPA TVLPDAILPE AGDCFLLCSD GLSGMISDRE IERIVSRQSE MGSQERVDYL VQRARDNGGL DNITVEIVEF SITPGSPSKP QRRKIGMIIL TVILLICIGA SGGYYFWNKH FKSESITIYK SFMRRDTIIM LPEIKFQKGE DILEINYKQG HTEILMGKEK EKVIEINRAL SSDSLKYDED IDVAYGNRLL VFRQEFKNEQ LRFSLADSVK IFKFVVPVVK DMTLTQPKQT HQESTPSVVN DVSNTANGSI VAIVAATGKV DSLTYRVDAQ FVPKRKAFSF IEGENACFLV EGQSQPSKLN RHFQITDIEY DATYFKKTKK ETGFDISFTE KEPPKKIDIV IKGKEKEGEN STDVLLNIII SLNINKEGK //