ID   Q6ABC1_CUTAK            Unreviewed;       495 AA.
AC   Q6ABC1;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=PPA0187 {ECO:0000313|EMBL:AAT81945.1};
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT81945.1, ECO:0000313|Proteomes:UP000000603};
RN   [1] {ECO:0000313|EMBL:AAT81945.1, ECO:0000313|Proteomes:UP000000603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT81945.1; -; Genomic_DNA.
DR   RefSeq; WP_002517157.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6ABC1; -.
DR   EnsemblBacteria; AAT81945; AAT81945; PPA0187.
DR   GeneID; 66620203; -.
DR   KEGG; pac:PPA0187; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_1_1_11; -.
DR   Proteomes; UP000000603; 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   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;
FT   DOMAIN          6..245
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   495 AA;  52759 MW;  514B2D5A97064E66 CRC64;
     MAFSLDIRCH SEIGLVRRNN QDSGYVSPRM LVVADGMGGA AAGDLASTVA VRHVAKADRR
     FSGEGSPARP QGEEMLTVLS GAVADANDEL ADLVAWDSSL EGMGTTFCGA MFSGTQLGIV
     HIGDSRGYLL RQGRMKRMTH DHSWVQSLID DGRITPEEAA VHPHRSLLLK VLNGQPQHIP
     DTQIVDLRLG DRILFCSDGL CGLVNDDTIG EHLNTTNLDD VVDLLTTDAH AGGGTDNITI
     VVAEVVEADP NLDASEPHII GAATTRKVPE HEVTAPLPLD QPASATNNDG KSTVLFDSEA
     EESMRYAPVD SMTRHRRHWL WPVVILAFVA VVVGGIFGAR AYLNTQYYVG TDDDTVAIYQ
     GSPDNLAWIQ LSHVTEKTNI KTADLPRYYR DRVLGNIRVS SMDSAHATVA ELRTGAQQCK
     VIREAATAPP PTKPATPPST PPQPSASGPT ANAHHTPQPS AVPTPAMPTP TSAMPSPSAA
     GHEVDLPAVT SGDCQ
//