ID   Q55726_SYNY3            Unreviewed;       691 AA.
AC   Q55726;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=sll0602 {ECO:0000313|EMBL:BAA10367.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA10367.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA10367.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10367.1; -; Genomic_DNA.
DR   PIR; S76521; S76521.
DR   AlphaFoldDB; Q55726; -.
DR   IntAct; Q55726; 2.
DR   STRING; 1148.gene:10499868; -.
DR   PaxDb; 1148-1001636; -.
DR   EnsemblBacteria; BAA10367; BAA10367; BAA10367.
DR   KEGG; syn:sll0602; -.
DR   eggNOG; COG0631; Bacteria.
DR   InParanoid; Q55726; -.
DR   PhylomeDB; Q55726; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001425};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        649..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          258..520
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          527..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          341..368
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        574..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..616
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  77764 MW;  E81CBBC39FEB03C9 CRC64;
     MPTVHCSNCD CQAPNDLGDR LCKTCRTPLL KRYLWSVGDW IKAYQPGELL LERYLLVRPQ
     VLLDTTPALG VEGPEEIPNY ILPYQKLLPF RLNVPEVYDY FPSWDEEKDL SVWLLDYGPV
     ALDQAGEPVH EQLLPSLGEM WEHACPLQQL TWLWQMIRLW QPLQRQGVVS SLLEFDWLRV
     QGPQVLLQQL KLDEHQFYEM KYLAGVWEPL LTNAHPAIAD FCQTLWKKLK QGKIPHADHL
     LRVLDTGIQS LAEQYDFSYT VFALTDGGPS RDHNEDACFP VSETPIEGQQ LANTMTLICD
     GVGGQEGGEI ASQWVIEHLP VRVISKIQKQ MNEPEQIRTF IQHLKEDIQE VNEQLNRRND
     REERTERERM GTTLVMALAD FQQFFLANVG DSRCYWLTAD SCKQVTVDDD VASREVRLGL
     MLYRHAVELP RSGALTQAVG LGPSAQLHPI IQRLIVPTDC LFLLCSDGFC DYNRVEQYWQ
     DDFLPVLQGD RPVAEAVPRL IELANQVNGH DNVSVALIHC QISPSVPTPT QAEKAAAEAE
     INDPEGDSPE EDFTGDTELG LKAIAYPDFS QRPVSKPKET EPEHPIPQQD PKESLASRPF
     DTQPPLPPEE IPLNPPLDPP TVMAEQLNKT HRSRSLAAKF LTLSKTSQLL IAGGMVIIIA
     TLTVAMLNLS QGNGEQNQPS SSLIDLSVGH G
//