ID   A4X0X9_SALTO            Unreviewed;       482 AA.
AC   A4X0X9;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Strop_0044 {ECO:0000313|EMBL:ABP52529.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS   105044 / CNB-440).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP52529.1, ECO:0000313|Proteomes:UP000000235};
RN   [1] {ECO:0000313|Proteomes:UP000000235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC   {ECO:0000313|Proteomes:UP000000235};
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP52529.1; -; Genomic_DNA.
DR   RefSeq; WP_011903966.1; NC_009380.1.
DR   AlphaFoldDB; A4X0X9; -.
DR   STRING; 369723.Strop_0044; -.
DR   KEGG; stp:Strop_0044; -.
DR   PATRIC; fig|369723.5.peg.44; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_1_1_11; -.
DR   Proteomes; UP000000235; 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:UP000000235};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        303..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..236
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          252..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..439
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..482
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  50038 MW;  24E0A03E54B17C1B CRC64;
     MTLTLRYAAH SDRGLIRDGN QDSVYAGPRL LAVADGMGGM AAGDVASNIV IGAMAPLDED
     VPGNALVDAL RSAVTNATQQ LRETVDANPQ LEGMGTTLTA ILFSGSKLGM VHIGDSRAYL
     LRASEFAQIT KDDTYVQMLV DEGRISAEEA SSHPQRSLLT RALDGRDIDA EYSVRQVLTG
     DRYLICSDGL SGVVSAETIA ETMREYADPQ QCVERLVQLA LRGGGPDNIT VIIADATDQD
     IVEATPIVGG AASRDRGMAT SADDSTPAAR ASALSGSPPV TPDESTAAAD EEPERRRRRP
     IRLVATSLAL IVLLGGALYG GWSYTQRQYY VGATGGGQVA VFRGIEGEIA GIDLSAVHST
     SSAELDDLTL AAQERVKQGI PAESEADAER RLAELTADTP TNPNLKPTCP PSPSPSPSPP
     VVPSPTAEPG APTPTTEPSA PPSISATSST PATGLPTEPT LSPDALPAIP PAVDPAACRS
     PE
//