ID   Q02BH5_SOLUE            Unreviewed;       862 AA.
AC   Q02BH5;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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_0585 {ECO:0000313|EMBL:ABJ81591.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ81591.1};
RN   [1] {ECO:0000313|EMBL:ABJ81591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ81591.1};
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; ABJ81591.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q02BH5; -.
DR   STRING; 234267.Acid_0585; -.
DR   KEGG; sus:Acid_0585; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_012906_0_0_0; -.
DR   InParanoid; Q02BH5; -.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 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:ABJ81591.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ81591.1};
KW   Transferase {ECO:0000313|EMBL:ABJ81591.1}.
FT   DOMAIN          12..275
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   862 AA;  91815 MW;  2E426E1B32A46723 CRC64;
     MALTGGEKLG PYEILSALGA GGMGEVYRAR DARLGRDVAL KVLPAEVASD PTRRQRFEIE
     ARAIAALNHP NIVAVYDVGS ESGVLYIVTE LVEGETLVGA KAGLRKTIEI AVQIAGGLAA
     AHEAGIVHRD LKPSNIVLAR DGRVKILDFG VAKVTPAIAA GAAITETITV NTRPGAVMGT
     VGYMSPEQVL GNSADHRSDI FSFGIILNEL LTGKRAFQGA TSVDTMQAIL RQDPPLLPET
     VPVPVRQIVQ HCLEKEPGNR FQSARDLAFA LSAYAQGSSQ SDLNTVLPAG SRTRRWRWSL
     LALPVAAALG ALAGGYWLNP AAPPTYTGML LGGPEVTMGP RLSPDGHILA FQAMVEGLTQ
     VAVMRPETGD WTALTHQRER GFVLEMSWAA DGSRIYYDRV TDVPRGVFSV PVLGGTEHLV
     LEDAMWPQAL PDGSLLVTRL NADRRQQLYH FWPESGRMEA IALLTPNFYA TVRASADGKR
     AFALGHPAGG GQAAQHLYAI DVASGSVRQL ATGLPNDSAM QALALTRDGK SLLVSLVAGN
     MGKVAKLPID GSGGARTLLT VSGHPEYIDS GPDESVYVDE HTTAMNSLRI KPASGRAQRD
     ATIPVAQLPS PFHAAVLGDG REVFAKYAGG RSRLMVFDGT KEAAPLVNTT EETAGPVAPV
     GESEIAFLVG PEPRRTIAMA TVRNGRITRR IGFDHGTINS LAATPDGKVL LCSAGGAVWR
     IPLTDGEPKR LRAGNAIALD AAGRNLFVQV IESPKTRLIR VPLDGGAEQE VPVQEPYHLS
     TNLIGPNAVG KDGQLVAPML SPDAWSSPPY LIDLATGNVK RLRVEGFDFA DYRFLGWGRD
     GEVVAAAFEL RSAMWKFVPE KR
//