ID   Q022E9_SOLUE            Unreviewed;       839 AA.
AC   Q022E9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
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_3174 {ECO:0000313|EMBL:ABJ84151.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84151.1};
RN   [1] {ECO:0000313|EMBL:ABJ84151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84151.1};
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000473; ABJ84151.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q022E9; -.
DR   STRING; 234267.Acid_3174; -.
DR   KEGG; sus:Acid_3174; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_012906_0_0_0; -.
DR   InParanoid; Q022E9; -.
DR   OrthoDB; 127317at2; -.
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; 2.120.10.30; TolB, C-terminal domain; 3.
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; IPR011659; PD40.
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; PF07676; PD40; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 2.
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:ABJ84151.1};
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:ABJ84151.1};
KW   Transferase {ECO:0000313|EMBL:ABJ84151.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        277..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..258
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   839 AA;  88414 MW;  2BA241FBB1089D28 CRC64;
     MPLKAGALLG PYEILALIGT GGMGEVWKAR DTRLKRTVAI KVSKSNFINR AEHEARAVAA
     LSHPNICMLY DIGPDYLVME YIEGKPLQGP MPVETALRHA IEIAKALDAA HRVGIIHRDL
     KPANILVTKS GIKLLDFGLA KVTAASAVSD ETVTRGLTEE GSILGTLQYM APEQLAGGEA
     DARSDIFAFG CVLYELLSGE PAFAAASRAG IIAAILEREP KALPAAPAHV AATLQRCLAK
     DPDDRWQSAR DLAGVLELAG GTAEIAAPPV RTSKRGLAAL AMLALLACAA AFWFGFRTPP
     NQFWSGQALG GPPRALGPRV SPDGHTLAFQ AMTDGQLQVA VMKPESGNWT VLTHQKDFGE
     LLSIAWSRDG SKLYFDRHSD SPRGVFSVPV LGGEPRLVLG GAYFPCVLAD GSLVVTMFNA
     QRIQQLFQYW PDSGKLEPLP ATPFGLSLGA LRGTPDGKAI LFYGNALDEK GAKGDRSLYL
     LDVASRKLVN VTPGETINGF IAAAATPDGR SVLYTKADNG FVSVISAPRG GSGPRRLLFT
     LTSTAWYLDV AADGSIYIDQ MAADNTLLRF SAQGGAVERL TEPQSQIPGN SGGLALVLPD
     GRPLVYNVAG LQRRMQIVQA GGSLSSLIEG NDDYGLPAAM AGVGSVALLT RRAPLEIVTV
     SIADGRIARR VAFQAEGTSS LASSPDGSTF YYNSGGYIWS MPAGGGAPHK LAAGEGVSAD
     PNGRDLLVAR QESDSVRLVR VGVRDGAEQP IVFRGGMRLA GTDLGAAAIG PGGMLAVKAI
     STDRWIYQVG LIDPRAGTIV PVPIGADIEA GVPTWTRDGK IVASGTTYDM SIWRFHPTP
//