ID   Q48JY5_PSE14            Unreviewed;       553 AA.
AC   Q48JY5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=PSPPH_2072 {ECO:0000313|EMBL:AAZ33647.1};
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ33647.1, ECO:0000313|Proteomes:UP000000551};
RN   [1] {ECO:0000313|EMBL:AAZ33647.1, ECO:0000313|Proteomes:UP000000551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA   Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA   Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA   Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ33647.1; -; Genomic_DNA.
DR   RefSeq; WP_011168362.1; NC_005773.3.
DR   AlphaFoldDB; Q48JY5; -.
DR   KEGG; psp:PSPPH_2072; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034273_0_0_6; -.
DR   Proteomes; UP000000551; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; PTHR43895; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE KINASE-RELATED; 1.
DR   PANTHER; PTHR43895:SF168; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 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   Kinase {ECO:0000313|EMBL:AAZ33647.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ33647.1};
KW   Transferase {ECO:0000313|EMBL:AAZ33647.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..224
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          257..515
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   553 AA;  61764 MW;  07FAF10FCF1EACE1 CRC64;
     MTLQLQFAQF SASGPRAENQ DALRLVTPAP TLAASKGYLF ALADGVSQCA DGALAAQSTL
     QALALDYYAT PETWGVAQSL DRLLLAQNRW LLANGLLTTL SALVLRGRRF TLAHVGDCRA
     YRWQAGTLKR ISEDHVWEQA DMQHVLKRAL GLDQYVVMDY LDGELCEGER LLLVSDGIWA
     TLGDASIRSI LTEQDDLDSA VKTLVSAAHL AGSQDNASAL LIQVDRLGED DLGDTLLQLQ
     QWPLPPALKA GQIFEGWTVG SIVAQSRQSI LYRVTDTHGQ PWLLKTLPAS RHDESGAGQG
     LLLEEWFLRR VAGRFFPEVH PLADRQHLYY VMREYCGNTL ADVFTRNGPL PLAQWQDLAT
     RLLRAAGLLH RRNIIHRDIK PENLLLADDG ELCLLDFGLA YCPGLSTGNA DDLPRTPSYI
     APEAFNGAEP HPQQDLYAAG VTLYYLLTGH YPYGEIEAFQ HRRFGTPIAA SRYRPDLPQW
     LSQSLDKALQ ADPHQRYETA EQWLLEMEQA EHRPVVAKPR PLLEREPLKV WQTLALISML
     LNLLLVIWLM SHH
//