ID   D2NQ69_ROTMD            Unreviewed;       588 AA.
AC   D2NQ69;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=RMDY18_19550 {ECO:0000313|EMBL:BAI65787.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI65787.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI65787.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI65787.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA   Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT   "Isolation and identification of Rothia mucilaginosa from persistent apical
RT   periodontitis lesions.";
RL   J Osaka Dent Univ 44:93-98(2010).
RN   [3] {ECO:0000313|EMBL:BAI65787.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI65787.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA   Fukushima H.;
RT   "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT   with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT   Lesion.";
RL   Sequencing 2010:457236-457236(2010).
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; AP011540; BAI65787.1; -; Genomic_DNA.
DR   RefSeq; WP_012904359.1; NC_013715.1.
DR   AlphaFoldDB; D2NQ69; -.
DR   STRING; 680646.RMDY18_19550; -.
DR   KEGG; rmu:RMDY18_19550; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_1_1_11; -.
DR   Proteomes; UP000001883; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        431..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..242
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          522..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  62512 MW;  E59D9311B95242DD CRC64;
     MKIAFRFEAR SDTGLKRSKN DDSGYGGRFL AVVADGMGGH VGGDVASATT VLNLTPLDHP
     DFEDGTGSVY LADEIQSANL IINELAANDP QLAGMGTTCT ALLIDGDCIE FAHIGDSRAY
     RLRPGADGEF EQISTDHTFV QRLLNEGRIT PQEAENHPHK NVIMRVLGDV DASPELELKT
     LDAVPGERWV LSSDGLDAVV SLAEIEQVMR STDDLSEIAD TLVAMTLERG APDNVTVVSL
     QVIDREVLPV DEPVGPSSLP ESALPDSIVA EQEVSTNTQK LPEVAATAEA AEAFLGAHHD
     EDSEEHHRRS LRRFRRARDF SGTLLHSGSG AVRHHIGTYD NAVDAALTNA AILRSELGSR
     PHQLVGAASV ATETGMIPAV TSRTLEHRAT VAQRVPLKVE SDEAALPAEL EELIAEDTEE
     RSRPRSWPIR LFITLLVAAV LTLAAWTGLR YVERSYYVGE SDGTVAVYNG IPHALGPIRL
     SHVVENTDIP TSELSDHTRS LLRNAITAKD LDDAHQIVSR LKTQADQTRE KAEQAAASAS
     ASASASPSSA APSEALSSGA PGSDSTSPAP ELATVSSAPA AEGGENNG
//