ID   Q024Y3_SOLUE            Unreviewed;       615 AA.
AC   Q024Y3;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Acid_2454 {ECO:0000313|EMBL:ABJ83443.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ83443.1};
RN   [1] {ECO:0000313|EMBL:ABJ83443.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ83443.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Janssen P.H., Kuske C.R., Richardson P.;
RT   "Complete sequence of Solibacter usitatus Ellin6076.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000473; ABJ83443.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q024Y3; -.
DR   STRING; 234267.Acid_2454; -.
DR   KEGG; sus:Acid_2454; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_444037_0_0_0; -.
DR   InParanoid; Q024Y3; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABJ83443.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ83443.1};
KW   Transferase {ECO:0000313|EMBL:ABJ83443.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          343..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   615 AA;  64444 MW;  25B24C0D2791ADBB CRC64;
     MIGRTISHYQ VTERLGSGGM GEIFKARDPR LNRTVAIKAL SIEGMGDPDR RRRFIQEAQA
     ASGLNHPNII TIHDIISDSE NEYMVMEYVS GKTLSELIQA GGVGVEKTLR YGVQMADALA
     AAHAAGIVHR DLKPGNVMVT ESGLVKILDF GLAKVSMATQ LTEETQTLGA PMTVEGSILG
     TVSYMSPEQA QGAKVDARSD IFAFGALMYE MITGTKAFSG ASPIATLTAI LRDEVKPVRD
     SVTDCPPELE EIIGRSLRKA PGDRWQSMQE VHGVLAALRQ KFESGILYGA KVVPVKKSAQ
     TLMLGLIAFL FVFGLGGWFI LIRRTQKSAP PPVPLAVQPA PAAAAPPVIP NDKPSPLAEA
     PKVEDPPKPA EPVKPAATAR RDGALTNQGV LELAAAKVPD AVIIGQIRGS KTRFDLSNPG
     VIALSKGGVS AAVIEVMRHP GDAPAATPLP VLPPAALPVP LAAAAPSKLA LAPVTAPGVS
     QRVAVVGGAA FEIVLMEDVP AEPVPGTPLR FQVGKDVVAG NSVVLARGAA VRGEVLEPGK
     KGGILRRGGK PAFRLMDAAA VDGSKLAIKA SPGRSGDKNE HNIEPPGHKS KELLASKGTV
     YLAYFDGDQT VAVKK
//