ID   B3PHD2_CELJU            Unreviewed;       587 AA.
AC   B3PHD2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 75.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
DE            EC=3.1.3.16 {ECO:0000256|PROSITE-ProRule:PRU01082};
GN   OrderedLocusNames=CJA_0329 {ECO:0000313|EMBL:ACE84098.1};
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Cellvibrionales; Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84098.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE84098.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84098.1,
RC   ECO:0000313|Proteomes:UP000001036};
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = 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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PROSITE-ProRule:PRU01082};
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DR   EMBL; CP000934; ACE84098.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PHD2; -.
DR   STRING; 498211.CJA_0329; -.
DR   KEGG; cja:CJA_0329; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034273_0_0_6; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACE84098.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..253
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          286..551
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   587 AA;  65474 MW;  DEB52358EBFC064E CRC64;
     MQHRSARLLI VYYPAMDHLQ SPLHISFAQK SDAGHKPENQ DTVGARLPDG NLLTTKGIAI
     AIADGVSSSK AAREASQTAI AGFLNDYYAT PDTWSTQQSA MRVIQALNSS LWGRSQNSIY
     GEGYLTTFSA LILKGASAFI FHVGDTRVYR LRDQHLELLT RDHTQRIDKH TTHLSRAMGA
     DPYLEVDMHS LELHAGDLFI LTSDGIHEAM PPQELRQLAI NQRNRLEVLV DQALQLALYH
     QSDDNLSIQA VSIENLGTAG QDDTLQVLSR LPFPPVLSPG QILDGLRIKK ILHESTRSQV
     YLVEDDQKNL LAMKTPSELF LDDPAYIERF VMEAWIGARI HSPGVVRVMA APESRSCLYY
     LTEYIPGPTL AQLLKERGIL SIVDAVELIE SLLRGIRAFH RKETLHQDLK PDNIVVGARG
     PVIVDFGSCW VASVQEAGAP IARDHILGTL DYSAPEYRYG ATPGTASDQF SLAVLLYEML
     TGKLPYGTGY SKAMDLKSFQ RLAYIPAMKH NPLVPYWLDK ALEKALSINP NHRYTALSEW
     LQDLKRPNPL WLTPRAQPLL ERDPLKAWKV IAISGWICAL VALLWRG
//