ID   Q7UFS9_RHOBA            Unreviewed;       485 AA.
AC   Q7UFS9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
DE            EC=3.1.3.16 {ECO:0000256|PROSITE-ProRule:PRU01082};
GN   Name=Pph1 {ECO:0000313|EMBL:CAD78601.1};
GN   OrderedLocusNames=RB8362 {ECO:0000313|EMBL:CAD78601.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC   Pirellulaceae; Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78601.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD78601.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294147; CAD78601.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7UFS9; -.
DR   STRING; 243090.RB8362; -.
DR   EnsemblBacteria; CAD78601; CAD78601; RB8362.
DR   KEGG; rba:RB8362; -.
DR   PATRIC; fig|243090.15.peg.4025; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_0_0; -.
DR   InParanoid; Q7UFS9; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   FunFam; 3.60.40.10:FF:000275; Protein serine/threonine phosphatase PrpC, regulation of stationary phase; 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; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 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:CAD78601.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        276..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..253
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          335..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  52177 MW;  20E110FFBD98A76C CRC64;
     MSGSWRPGVK FAEQTHVGMR RANNQDSSAV LIAESAERLN QRGHLFVVAD GMGAHAAGEL
     ASQIASERIS MHYYQSREEA PEHAISEAVH LANAAIYERG QSNPEFLNMG TTASSLVLVN
     GAAYVAHVGD SRVYRLRQGV LEQLTFDHSL VWEMQASGKV HSDSVFSKSI PKNVITRSLG
     PSPEVLVDLE GPFDLEVGDR FMVCSDGLTG QIEDDELAVL LDSLDVDKAA RVMIDLANLR
     GGPDNITLIV VEVDDEHLTQ NDGAPRKARS LGADEVSSRA LIGTTAFCWT GAVGFGLAAA
     LVSPRFVGSA IVAFILGSIS AAVWASGVFK PNERRRPLKT RRVRDRNSAG ASSNPGMPGQ
     SGAGQGGSSD PALAGDAWDS GESLDIGSGE TALGTGPYRR FKANSHEAFL LRMDDVITQL
     RQTSEERNWM LDWQNVDQLL QQARQATKEQ AWGTAVSSYC DATLAAMEQL RKHQDDSASD
     TVVDL
//