ID   Q883P7_PSESM            Unreviewed;       529 AA.
AC   Q883P7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   SubName: Full=Serine/threonine protein kinase, putative {ECO:0000313|EMBL:AAO55817.1};
GN   OrderedLocusNames=PSPTO_2303 {ECO:0000313|EMBL:AAO55817.1};
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO55817.1, ECO:0000313|Proteomes:UP000002515};
RN   [1] {ECO:0000313|EMBL:AAO55817.1, ECO:0000313|Proteomes:UP000002515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA   Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA   Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA   D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA   Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA   Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; AE016853; AAO55817.1; -; Genomic_DNA.
DR   RefSeq; NP_792122.1; NC_004578.1.
DR   AlphaFoldDB; Q883P7; -.
DR   STRING; 223283.PSPTO_2303; -.
DR   KEGG; pst:PSPTO_2303; -.
DR   PATRIC; fig|223283.9.peg.2339; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034273_0_0_6; -.
DR   OrthoDB; 9801841at2; -.
DR   PhylomeDB; Q883P7; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00143; PP2Cc; 1.
DR   CDD; cd14014; STKc_PknB_like; 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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; 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.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAO55817.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002515};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:AAO55817.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..200
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          233..491
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   529 AA;  59243 MW;  3FC64090689ECA1C CRC64;
     MVTPTPALAA SKGYLFALAD GVSQCADGAL AAQSTLQALA LDYYSTPETW GVAQSLDRLL
     LAQNRWLLAN GLLTTLSALV LRGRRFTLAH VGDCRAYRWQ AGTLKRISED HVWEQADMQH
     VLKRALGLDQ YVVMDYLDGE LCEGERLLLV SDGIWATLGD ASIRSILTEQ DDLDSAVKTL
     VSAAHLAGSQ DNASALLIQV DSLGTDDLGD TLLQLQQWPL PPTLKVGQTF EGWNVGDIVA
     QSRQSILYRV KDAHGQPWLL KTLPTSRHDE AGAGQGLLLE EWFLRRVAGR FFPEVHSLAQ
     RQHLYYVMRE YPGSTLAEVF RRNGPLPLVQ WQDLATRVLR ATGLLHRRNI IHRDIKPENL
     LLGNDGELRL LDFGLAFCPG LSATNAEDLP GTPSYIAPEA FNGAEAHPRQ DLYAVGVTLY
     YLLTGHYPYG EIEAFQHRRF GTPIPASRYR PDLPQWLSQS LDKALQADPD QRYETPEQWL
     LELEQAEHRS LVTRPRPLLE REPLKVWRTL ALVSLLCNLL AVIWFMGRH
//