ID   Q021S6_SOLUE            Unreviewed;       845 AA.
AC   Q021S6;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
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_3325 {ECO:0000313|EMBL:ABJ84299.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84299.1};
RN   [1] {ECO:0000313|EMBL:ABJ84299.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84299.1};
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; ABJ84299.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q021S6; -.
DR   STRING; 234267.Acid_3325; -.
DR   KEGG; sus:Acid_3325; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_012906_0_0_0; -.
DR   InParanoid; Q021S6; -.
DR   OrthoDB; 100367at2; -.
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; 2.120.10.30; TolB, C-terminal domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 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:ABJ84299.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ84299.1};
KW   Transferase {ECO:0000313|EMBL:ABJ84299.1}.
FT   DOMAIN          12..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   845 AA;  89859 MW;  6DBC7B72E75F0E34 CRC64;
     MPLSAGARFG PYEIRAPLGA GGMGEVYRAR DTRLGRDVAL KILPPELAED PSRRARFEQE
     ARAVAALNHP NIVAVFDVGD GYMVSELVEG EPLRASHPGL RKTLDLAGQI ASGLAAAHAA
     GIVHRDLKPE NVLVTKDGRA KILDFGLARI RRNAAVASGQ TETATVKTEP GTVMGTVGYM
     SPEQVRGLEA DHRSDIFSFG VMLHEMLAGT RPFLGETSVE TMMAILKQDA PDLPGSVPET
     VRTIVEHCLE KEPANRFQSA KDLGFALAQS TSRSDSAPVL AARPGNRRRA ALAAALMVLS
     AAATWWLSHG TPATQWTAVE LGGPEIALSP RLSPDGHVLA MLAMVDGNTQ VAVMKPETGS
     WNVLTHSRDQ GMVTHLSWSQ DGASIYYSRL TDVPQGVFSV PFLGGEEHLV LENAANPAVL
     QDGTVVLSRL NGQNHPQLFR FWPETGKLQE LPVQPDDMRD HQVSRDGRHA VVTGAIYGKA
     GKSSLIEVDL LRATARVIPT PELDWLTFAG MALSPDGRSV LMSARSNTLS RVIRVPLDGG
     ARPQDLFRVT STIWGLDAAA DGSVLANLVD RPTELVSFPA TGGPAVKIAG FRETPEWDMV
     VALPDGRAVT PVEVAGLTRL IAVAPGKTPS PLIQTPEATT SPVTAVGADR IAFLIGPEPH
     DTIAIANTSN GRIGMRIAPG KGMIESLAAS PDGGTLYFGA GGSIWSVASS GGEGRRICPG
     SWVVTAPWGG LIVARTEIAQ IRLFELPAGG GPERAIPVNR TSPLLSLFIT PGTIRADRRM
     LVSLNVADSW FNPLALLDLD SGKVTRIAGD GVSDLHSGAW SRDGRILASR KGMQGTIWRF
     TPEVR
//