ID   Q9CDE5_MYCLE            Unreviewed;       509 AA.
AC   Q9CDE5;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=ML0020 {ECO:0000313|EMBL:CAC29528.1};
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC29528.1, ECO:0000313|Proteomes:UP000000806};
RN   [1] {ECO:0000313|EMBL:CAC29528.1, ECO:0000313|Proteomes:UP000000806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN {ECO:0000313|EMBL:CAC29528.1,
RC   ECO:0000313|Proteomes:UP000000806};
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583917; CAC29528.1; -; Genomic_DNA.
DR   PIR; D86911; D86911.
DR   RefSeq; NP_301146.1; NC_002677.1.
DR   RefSeq; WP_010907471.1; NC_002677.1.
DR   AlphaFoldDB; Q9CDE5; -.
DR   SMR; Q9CDE5; -.
DR   STRING; 272631.gene:17573831; -.
DR   KEGG; mle:ML0020; -.
DR   PATRIC; fig|272631.5.peg.24; -.
DR   Leproma; ML0020; -.
DR   eggNOG; COG0631; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   HOGENOM; CLU_025431_0_0_11; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000806};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        300..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..235
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          418..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..438
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  53577 MW;  6D0B3DF76D9D1ED9 CRC64;
     MTLVLRYAAR SDRGLVRANN EDSVYAGARL LALADGMGGH AAGEVASQLV IAALAHLDDD
     EPGGDLLGKL ETAVRAGNLA IAAQVEMEPD FEGMGTTLTA ILFAGNRLGL VHIGDSRGYL
     LRDGELTQIT KDDTFVQTLV DEGRITAEEA HSHPQRSLIM RALTGHEVDP TLTMREARAG
     DRYLLCSDGL SDPVSDETIL EALQIPDVAE SAYRLIELAL RGGGPDNVTV VVADVIDYDY
     GQTQPILAGA VSGEESQQMA LPNTAASRAS AIVPRKEIAK SMAPQVDKVH QQRWSQRQTG
     ITLTLLVLLV LAGVAIGRWV IRDNYYIAEY SGKVSIVRGI QGSLLGMPLH EPYLVGCLNT
     RNELSLISYG QSGGHLNCQV MTLRDLRPSG GAQVQAGLPG GNLDQAESQL RKLLADSLLP
     TCPPPRATSP PGPFTMPTDS GTPQPTNTAS PTSTTPPTIT SSSGTAPTNI SPTSSPASTA
     PTTPVGTSQT VTILPPPPPQ PGIDCRAVA
//