ID   STP1_LISMO              Reviewed;         252 AA.
AC   Q8Y678;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Serine/threonine phosphatase stp;
DE            EC=3.1.3.16;
GN   Name=stp; OrderedLocusNames=lmo1821;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   FUNCTION AS PHOSPHATASE, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, DISRUPTION PHENOTYPE, AND IDENTIFICATION OF SUBSTRATE.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=15813732; DOI=10.1111/j.1365-2958.2005.04551.x;
RA   Archambaud C., Gouin E., Pizarro-Cerda J., Cossart P., Dussurget O.;
RT   "Translation elongation factor EF-Tu is a target for Stp, a serine-
RT   threonine phosphatase involved in virulence of Listeria monocytogenes.";
RL   Mol. Microbiol. 56:383-396(2005).
CC   -!- FUNCTION: Protein phosphatase that dephosphorylates EF-Tu.
CC       {ECO:0000269|PubMed:15813732}.
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   -!- 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:15813732};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:15813732};
CC   -!- ACTIVITY REGULATION: Activity not affected by inhibitors of
CC       phosphatases of the PPP family such as okadaic acid and cypermethrin,
CC       or by inhibitors of phosphatases of the PTP family such as sodium
CC       orthovanadate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.77 uM for MBP {ECO:0000269|PubMed:15813732};
CC         KM=0.62 uM for EF-Tu {ECO:0000269|PubMed:15813732};
CC         Vmax=120.48 pmol/min/ug enzyme toward MBP
CC         {ECO:0000269|PubMed:15813732};
CC         Vmax=2.94 pmol/min/ug enzyme toward EF-Tu
CC         {ECO:0000269|PubMed:15813732};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15813732}. Membrane
CC       {ECO:0000269|PubMed:15813732}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15813732}.
CC   -!- DISRUPTION PHENOTYPE: The stp-disrupted strain is 4 times less virulent
CC       than the wild strain, demonstrating that stp is required for full
CC       virulence of L.monocytogenes in BALB/c mice.
CC       {ECO:0000269|PubMed:15813732}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AL591981; CAC99899.1; -; Genomic_DNA.
DR   PIR; AE1302; AE1302.
DR   RefSeq; NP_465346.1; NC_003210.1.
DR   RefSeq; WP_003723065.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y678; -.
DR   SMR; Q8Y678; -.
DR   STRING; 169963.lmo1821; -.
DR   PaxDb; Q8Y678; -.
DR   EnsemblBacteria; CAC99899; CAC99899; CAC99899.
DR   GeneID; 985901; -.
DR   KEGG; lmo:lmo1821; -.
DR   PATRIC; fig|169963.11.peg.1866; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   OMA; MLNAQFF; -.
DR   PhylomeDB; Q8Y678; -.
DR   BioCyc; LMON169963:LMO1821-MON; -.
DR   BRENDA; 3.1.3.16; 15002.
DR   SABIO-RK; Q8Y678; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Manganese; Membrane; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..252
FT                   /note="Serine/threonine phosphatase stp"
FT                   /id="PRO_0000363063"
FT   DOMAIN          2..242
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   252 AA;  28026 MW;  47EE5DA232A43338 CRC64;
     MHAEFRTDRG RIRHHNEDNG GVFENKDNQP IVIVADGMGG HRAGDVASEM AVRLLSDAWK
     ETTALLTAEE IETWLRKTIQ EVNKEIVLYA ESEMDLNGMG TTLVAAIMAQ SQVVIANVGD
     SRGYLLQNHV LRQLTEDHSL VHELLRTGEI SKEDAMNHPR KNILLRALGV EGKVEVDTFV
     VPFQTSDTLL LCSDGLTNMV PETEMEEILK SKRTLSEKAD VFITKANSYG GEDNITVLLV
     ERDLTQKGRD AS