ID   Q3IWI9_CERS4            Unreviewed;       248 AA.
AC   Q3IWI9;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   04-NOV-2026, entry version 103.
DE   SubName: Full=Protein phosphatase 2C {ECO:0000313|EMBL:ABA81095.1};
DE            EC=3.1.3.16 {ECO:0000313|EMBL:ABA81095.1};
GN   ORFNames=RSP_3492 {ECO:0000313|EMBL:ABA81095.1};
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943 {ECO:0000313|EMBL:ABA81095.1, ECO:0000313|Proteomes:UP000002703};
RN   [1] {ECO:0000313|Proteomes:UP000002703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1. {ECO:0000313|Proteomes:UP000002703};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = 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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PROSITE-ProRule:PRU01082};
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DR   EMBL; CP000144; ABA81095.1; -; Genomic_DNA.
DR   RefSeq; WP_011339357.1; NC_007494.2.
DR   AlphaFoldDB; Q3IWI9; -.
DR   STRING; 272943.RSP_3492; -.
DR   EnsemblBacteria; ABA81095; ABA81095; RSP_3492.
DR   GeneID; 48981558; -.
DR   KEGG; rsp:RSP_3492; -.
DR   PATRIC; fig|272943.9.peg.3933; -.
DR   eggNOG; COG0631; Bacteria.
DR   OMA; AACIMGK; -.
DR   OrthoDB; 9801841at2; -.
DR   PhylomeDB; Q3IWI9; -.
DR   Proteomes; UP000002703; Chromosome 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
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; PTHR13832:SF827; PROTEIN PHOSPHATASE 1L; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082,
KW   ECO:0000313|EMBL:ABA81095.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002703}.
FT   DOMAIN          17..245
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   248 AA;  25532 MW;  D6F6BD55040499A3 CRC64;
     MKAPTTVVPR AGLRVEGWGI THRGHRRARN EDAILTDPAG QLWAVADGMG GHGQGDVAAD
     IVIDHLETIP EGGEPRRMLV AGLEAANAAI RAHARKAEVG QMGATVVALL IARTTAHVAW
     VGDSRAYLLR AGRLSALTRD HSVVQALVDA GHLDPAAAAL HPEANLVTRA VGASDTVEVE
     TVALEIAAGD RLLLCSDGLT HCVADPVLEG HLASAVGPYE SCLALVRAAL DAGGPDNVSV
     VVVDVAEG
//