ID   B8GNV1_THISH            Unreviewed;       276 AA.
AC   B8GNV1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Tgr7_0952 {ECO:0000313|EMBL:ACL72040.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL72040.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL72040.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL72040.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL72040.1; -; Genomic_DNA.
DR   RefSeq; WP_012637524.1; NC_011901.1.
DR   AlphaFoldDB; B8GNV1; -.
DR   STRING; 396588.Tgr7_0952; -.
DR   KEGG; tgr:Tgr7_0952; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_6; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000002383; 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   NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000002383}.
FT   DOMAIN          8..255
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   276 AA;  30316 MW;  EB036B8B3BA7D6A5 CRC64;
     MNDTAPILVA SRTDTGHVRS HNEDAIGNDP HLGVVVLADG MGGYSSGEVA SQIAVNTILD
     ELQRVLPGLN PGELDPELGY TRQTMAVREA ILRANHKIYQ AAQQDTRHAG MGTTLVMAAF
     HGNQVTIAHV GDSRLYRMRD RRLEQLTTDH TLIQELVDHG YYNREEARTA QNKNLVTRAL
     GIEPSVAVDV LEGLALPGDV YLLCSDGLND MIDDSTIERT LLEAAPDIEA AAERLVERAL
     NSGGRDNVSV VLTRVLDTHP KDLPWYKRIT KILKRS
//