ID   A7NLS5_ROSCS            Unreviewed;       422 AA.
AC   A7NLS5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   04-NOV-2026, entry version 84.
DE   SubName: Full=Protein serine/threonine phosphatase {ECO:0000313|EMBL:ABU58473.1};
GN   OrderedLocusNames=Rcas_2391 {ECO:0000313|EMBL:ABU58473.1};
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Roseiflexineae; Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU58473.1, ECO:0000313|Proteomes:UP000000263};
RN   [1] {ECO:0000313|EMBL:ABU58473.1, ECO:0000313|Proteomes:UP000000263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) 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; CP000804; ABU58473.1; -; Genomic_DNA.
DR   RefSeq; WP_012120897.1; NC_009767.1.
DR   AlphaFoldDB; A7NLS5; -.
DR   STRING; 383372.Rcas_2391; -.
DR   KEGG; rca:Rcas_2391; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_741544_0_0_0; -.
DR   OMA; ACCDRGI; -.
DR   OrthoDB; 152713at2; -.
DR   Proteomes; UP000000263; 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:UP000000263}.
FT   DOMAIN          163..417
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   422 AA;  45373 MW;  28C5B8158185A4F1 CRC64;
     MPRSRFCPTC GQALPQAALP FSAAPLLDVS DPPVEGVLTN GKRFHVSSDA LDLRELLHVV
     ESSVQWWQRG LTSSNAVTRE QAARAIDDLS QIMHSLSQQL AQGRTTIRVT RRLPVLRAFD
     VACPSCGCGN RAGARFCQRC GALLQAAPRY GVGSVQSRLL SFQIVARTDT GRVRQQNQDA
     VYAGEIDLPG QKKAYLCLVA DGMGGAAAGE YASRLAADVS RTYLERESAS HPPPTDDAWQ
     TLLRDAVRAA NRRIYDAAHA DSARRGMGTT LTIALLVGDR LHIASVGDSR AYLLNLHGVT
     DDGAPSAQLT SDHSLVARLV DIGQLTPEQA RTHPQRNILY RSIGTDPSVD VDTRSEALEP
     GDIVLLCSDG LVNHVSDEEI AQIALGESDL ERAATRLISL ANERGGRDNI SVVMVRVASD
     TG
//