ID   A4VNP6_STUS1            Unreviewed;       349 AA.
AC   A4VNP6;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=PST_2951 {ECO:0000313|EMBL:ABP80597.1};
OS   Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=379731 {ECO:0000313|EMBL:ABP80597.1, ECO:0000313|Proteomes:UP000000233};
RN   [1] {ECO:0000313|EMBL:ABP80597.1, ECO:0000313|Proteomes:UP000000233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501 {ECO:0000313|EMBL:ABP80597.1,
RC   ECO:0000313|Proteomes:UP000000233};
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP80597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VNP6; -.
DR   KEGG; psa:PST_2951; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_6; -.
DR   Proteomes; UP000000233; 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; PF00481; PP2C; 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:UP000000233}.
FT   DOMAIN          102..325
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   349 AA;  37587 MW;  877A4F5E555E2EF6 CRC64;
     MRRHRIAESG RHGQHVCVRA QPIALSKRLF AFRRSGKAAR SAGRESRNTA SGTLPPLREL
     TVLRLPRCQP MTASRAQRIM LARCHAAAGP RMQPTLSDSL LDYAGNSSPG RRRSHNEDAL
     LCAPTLGLWA IADGMGGHQC GEVASSLALV ALRQAVEDGE PLESAVHLAN QAVLETATDD
     GMGTTLVAAH FNGSDFELAW VGDSRAYLVS ADGIAQLTRD HSWVQMMIDA GELEPAAAQG
     HAWRNIILRC LGRETPLEVG IAAGSLKPDE LLLLCSDGLT NELTDAQIQA SCTFADTLEN
     LVEQLIEQAN AHGGRDNISC IVIGRTAQPQ ATESRGRRFI NMLLKPLKS
//