ID   B8I260_RUMCH            Unreviewed;       241 AA.
AC   B8I260;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Ccel_1534 {ECO:0000313|EMBL:ACL75886.1};
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503 {ECO:0000313|EMBL:ACL75886.1, ECO:0000313|Proteomes:UP000001349};
RN   [1] {ECO:0000313|EMBL:ACL75886.1, ECO:0000313|Proteomes:UP000001349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10
RC   {ECO:0000313|Proteomes:UP000001349};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP001348; ACL75886.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8I260; -.
DR   STRING; 394503.Ccel_1534; -.
DR   KEGG; cce:Ccel_1534; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000001349; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000001349}.
FT   DOMAIN          2..241
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   241 AA;  26799 MW;  3B307DBF736341E4 CRC64;
     MKYGIKTDRG LKRQLNEDNC NVLVGYPGIP VCFVIADGMG GHQCGDVASK QAVDSVCNHL
     LKSDWTTEGI PELLKNIIAT VNDEIYKFSL LDNSTQGMGT TLIITILKNR KLYIGHVGDS
     RVYLIRNNTI KKVTWDHSFI EEMLKNGSIT KDEAINHPKK NLITRAVGYE PDLQVDTYEI
     DVVENDFILL CTDGLTNMIT EDEILDIIIN TKDPQDACDT LIQNANNKGG EDNVTVIIGK
     I
//