ID   B2GHD4_KOCRD            Unreviewed;       527 AA.
AC   B2GHD4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=pstP {ECO:0000313|EMBL:BAG30410.1};
GN   Synonyms=ppp {ECO:0000313|EMBL:BAG30410.1};
GN   OrderedLocusNames=KRH_20630 {ECO:0000313|EMBL:BAG30410.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30410.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30410.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(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; AP009152; BAG30410.1; -; Genomic_DNA.
DR   RefSeq; WP_012399131.1; NC_010617.1.
DR   AlphaFoldDB; B2GHD4; -.
DR   STRING; 378753.KRH_20630; -.
DR   KEGG; krh:KRH_20630; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_0_0_11; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:BAG30410.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..239
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          243..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  55661 MW;  D0E2B6D847278D22 CRC64;
     MPIAFRYAAR SDVGRVRSKN DDSAYAGRYL AVVADGMGGH VGGDVASASA VIDLTHLDHA
     GHRGEAETVL ADEIQNANQN LAKLVQSNPR LGGMGTTVTA LLIDGDEISV AHIGDSRAYR
     LSETEGFQQV TTDHTFVQRL IDEGRLQPEE AETHPHKNVL MRVLGDVDAS PELEVRVVRP
     AVGERWLLCS DGLNAVVNAR TIENVMRSTG DLNQIVNSLV ELTLDRGAPD NVTVVVVQVD
     EIPPGDEAHP MTGEGHGAIP DESRTSDERL RVETVEEHWD GPMDSPVAGG GVDYREPGRQ
     EPPAPPEPAQ SSASVLRQDL AERPHLLVGA AANATQTGRI PTVSDSAMAR RATMLSTSTL
     DETTDPAEVR SLLRRKGEDP APASTRRRAV WVAGAVVLAV ALMLGGWGAR AWTSSQYYVG
     EDQGRVAVYQ GVSQSLGPIS LSDLDSTTDV RVDSLSQYAQ ERVRATIPAG SRDEAEKIVS
     ELKTSSGPGP HPTGRVTVTT PTPDPSSSAS GSGSPSPSAS ASGGGDS
//