ID   Q6MDA5_PARUW            Unreviewed;       259 AA.
AC   Q6MDA5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN   ORFNames=PC_RS03460 {ECO:0000313|EMBL:CAF23444.1};
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Parachlamydiales;
OC   Parachlamydiaceae; Candidatus Protochlamydia.
OX   NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF23444.1, ECO:0000313|Proteomes:UP000000529};
RN   [1] {ECO:0000313|EMBL:CAF23444.1, ECO:0000313|Proteomes:UP000000529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25 {ECO:0000313|EMBL:CAF23444.1,
RC   ECO:0000313|Proteomes:UP000000529};
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF23444.1; -; Genomic_DNA.
DR   RefSeq; WP_011175270.1; NC_005861.2.
DR   AlphaFoldDB; Q6MDA5; -.
DR   STRING; 264201.pc0720; -.
DR   KEGG; pcu:PC_RS03460; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_3_2_0; -.
DR   OMA; AADCYSG; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000000529; Chromosome.
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   NCBIfam; NF033484; Stp1_PP2C_phos; 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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000529}.
FT   DOMAIN          12..249
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   259 AA;  28842 MW;  5D96370E7D32E05A CRC64;
     MALQAMFYKT LVYGISDVGL VRQNNEDSWG QILEDHFFVL ADGMGGHRAG EVASKEAVSQ
     LCAKFKEKFS RCSKDIKSSF EMIKESIQEV NYNIYKMGRE QEILRGMGTT LCCVCLHSEG
     VIFGHVGDSR IYRLRDNNLK QITQDHSLLR ELIELGQLSE HQACEFAYKN IITKAIGTGP
     FVEPSLKIDS IEVGDVILMC TDGLSDLLSI QDIQQILSDT PDDEVTKKLV KVAKSRGGHD
     NITVVVIKVQ GKYESASLS
//