ID   A4G6X7_HERAR            Unreviewed;       309 AA.
AC   A4G6X7;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=HEAR2127 {ECO:0000313|EMBL:CAL62264.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL62264.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL62264.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(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; CU207211; CAL62264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G6X7; -.
DR   STRING; 204773.HEAR2127; -.
DR   KEGG; har:HEAR2127; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_5_0_4; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000006697; 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   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:UP000006697}.
FT   DOMAIN          2..243
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   309 AA;  34511 MW;  7BEF7DA053D35DBD CRC64;
     MRFSVYQESH IGGRKNNQDR MGYSFTRDAL LLLVADGMGG HIMGEMAAQI AMQTIASLFQ
     ENATPYVKKP ERFLEDSFFA AHREIHRYRA INNLPETPRT TIVACLIQHN SAMWAHCGDS
     RLYWMRGGQI LARTRDHSRI ETLIAQGKVD ASERETHPDR NKLFNCLGAP NMPIVEISRR
     VSLQAGDVML LCSDGLWSVL PDHELAQRLH SNTIVRAIPE LLSTATGIAG KTGDNVTALA
     MMWESSENLQ GNSTITTHTL PIGSVTTTIQ APRHLDLENA DTYNDSEIEK AIEEIRNAID
     KSSRITSRN
//