ID   Q8F681_LEPIN            Unreviewed;       269 AA.
AC   Q8F681;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=ptc1 {ECO:0000313|EMBL:AAN48627.1};
GN   OrderedLocusNames=LA_1428 {ECO:0000313|EMBL:AAN48627.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN48627.1, ECO:0000313|Proteomes:UP000001408};
RN   [1] {ECO:0000313|EMBL:AAN48627.1, ECO:0000313|Proteomes:UP000001408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 {ECO:0000313|EMBL:AAN48627.1,
RC   ECO:0000313|Proteomes:UP000001408};
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA   Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA   Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA   Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA   Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA   Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN48627.1; -; Genomic_DNA.
DR   RefSeq; NP_711609.1; NC_004342.2.
DR   RefSeq; WP_000636852.1; NC_004342.2.
DR   AlphaFoldDB; Q8F681; -.
DR   STRING; 189518.LA_1428; -.
DR   PaxDb; 189518-LA_1428; -.
DR   EnsemblBacteria; AAN48627; AAN48627; LA_1428.
DR   GeneID; 61142203; -.
DR   KEGG; lil:LA_1428; -.
DR   PATRIC; fig|189518.3.peg.1422; -.
DR   HOGENOM; CLU_034545_0_2_12; -.
DR   InParanoid; Q8F681; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000001408; Chromosome I.
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   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:UP000001408}.
FT   DOMAIN          33..249
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   269 AA;  29514 MW;  1F3023B0F42349FC CRC64;
     MIVNYFGITE KGNFRSHNED SMYVSGEIVA GTVSGSFSSS GMREAPLILA LADGMGGHIS
     GEIASRMTLE KLAWTERAVQ PLDELSRAGW QSLFSIINHE INDYAKETGK LGMGATLVGI
     LFGKRKVLVF NMGDSRAYHF SSQGIQKITV DHSFAGPVKE NQVSRSYITS CIGGGTTDLQ
     MDLFDITNSL NVGDRILLCT DGLTDVIKID DLEEILKNSS NAKEACYHLL EEANLRMTKD
     NTSVIVIEVQ EIILSNSKPW KLTPGEKKR
//