ID   Q9I757_PSEAE            Unreviewed;       242 AA.
AC   Q9I757;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=pppA {ECO:0000313|EMBL:AAG03465.1};
GN   OrderedLocusNames=PA0075 {ECO:0000313|EMBL:AAG03465.1};
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG03465.1, ECO:0000313|Proteomes:UP000002438};
RN   [1] {ECO:0000313|EMBL:AAG03465.1, ECO:0000313|Proteomes:UP000002438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA   Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA   Hancock R.E., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2] {ECO:0007829|PDB:6JKV}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH MN(2+).
RX   PubMed=31208722; DOI=10.1016/j.bbrc.2019.06.020;
RA   Wu Y., Gong J., Liu S., Li D., Wu Y., Zhang X., Ren Y., Xu S., Sun J.,
RA   Wang T., Lin Q., Liu L.;
RT   "Crystal structure of PppA from Pseudomonas aeruginosa, a key regulatory
RT   component of type VI secretion systems.";
RL   Biochem. Biophys. Res. Commun. 516:196-201(2019).
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; AE004091; AAG03465.1; -; Genomic_DNA.
DR   PIR; E83637; E83637.
DR   RefSeq; NP_248765.1; NC_002516.2.
DR   RefSeq; WP_003106965.1; NZ_QZGE01000015.1.
DR   PDB; 6JKV; X-ray; 2.10 A; A/B=1-242.
DR   PDBsum; 6JKV; -.
DR   AlphaFoldDB; Q9I757; -.
DR   SMR; Q9I757; -.
DR   STRING; 208964.PA0075; -.
DR   PaxDb; 208964-PA0075; -.
DR   DNASU; 879341; -.
DR   GeneID; 879341; -.
DR   KEGG; pae:PA0075; -.
DR   PATRIC; fig|208964.12.peg.78; -.
DR   PseudoCAP; PA0075; -.
DR   HOGENOM; CLU_034545_0_3_6; -.
DR   InParanoid; Q9I757; -.
DR   OrthoDB; 9801841at2; -.
DR   PhylomeDB; Q9I757; -.
DR   BioCyc; PAER208964:G1FZ6-77-MONOMER; -.
DR   BRENDA; 3.1.3.16; 5087.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:PseudoCAP.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IMP:PseudoCAP.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6JKV}; Metal-binding {ECO:0007829|PDB:6JKV};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002438}.
FT   DOMAIN          8..241
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   BINDING         41
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:6JKV"
FT   BINDING         41
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:6JKV"
FT   BINDING         42
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:6JKV"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:6JKV"
FT   BINDING         232
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:6JKV"
SQ   SEQUENCE   242 AA;  25904 MW;  1C13B17B31D03921 CRC64;
     MVPNSVSYYR SASYSHVGMV RKVNEDASLD APEAGLWVVA DGMGGHAAGD FVSSLIVDTL
     RRIPAASSLP AYVGALRTGL AQVNERVRQE AGLRGVSVMG STLVLLAARG NQASCLWAGD
     SRLYRLRGGV LEAISRDHSY VQELLDNALI SEEEARHHPR ANVVTRAVGV HEQLELSEAA
     LHVLPGDSFL LCSDGLNKTA DDSELRDVLS HSDPYAVVRS LVHLGLTRGA PDNITALVVR
     AF
//