ID   Q01P82_SOLUE            Unreviewed;       849 AA.
AC   Q01P82;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
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_7636 {ECO:0000313|EMBL:ABJ88538.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ88538.1};
RN   [1] {ECO:0000313|EMBL:ABJ88538.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ88538.1};
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; ABJ88538.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01P82; -.
DR   STRING; 234267.Acid_7636; -.
DR   KEGG; sus:Acid_7636; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_012906_0_0_0; -.
DR   InParanoid; Q01P82; -.
DR   OrthoDB; 100367at2; -.
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; 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; 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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 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; 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:ABJ88538.1};
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:ABJ88538.1};
KW   Transferase {ECO:0000313|EMBL:ABJ88538.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        298..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..281
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   849 AA;  90839 MW;  1C1BD37D16436FA5 CRC64;
     MPLSAGDKLG PYEVVAPLGA GGMGEVYKAN DPRLARSVAI KVLPESLARD GDRLRRFEIE
     AKAAGGLNHS NILVVHDIGT ENGVPYLVSE LLDGESLRAR LTLGKIPTTR AVELARQIAS
     GLAAAHARGI VHRDIKPDNL FLTRDGRVKI LDFGLAKVTP GEVVTDATRT LHTSAGTVLG
     TVSYMSPEQV RGQTVDHRSD IFSFGAVLLE MLTGEKAFAA PTAADTMSAI LNSDPAISPE
     DEAAIPTAHL RTIRHCLEKN ADDRFQTCKD LAFDLESATA LGTVSSFRRT LPKRRIRMPA
     WAIAVAASAI AAAAVWWAIA KPSIQPAFQR LTFRRGIVQS ARFGPDGRTV VYAAAWNGQP
     VELYSVQPGS PESRPLELKS TGLLGVSKSG ELALLVACRF QGAFLTVGTL AQAPLNGGAP
     RELLDEVAYA DWSPDGTQMA VSTYAKPRRI EYPVGTRLFT APGSAWPGEV RISPKGDRIA
     FADHYYYGDD GSVAVVNLQG EKKTLSSKFN SLQGIAWSPD GDEVWFTGAK NGGQRAVYAV
     TLGGKERLIF RAPGAVKLHD VGRDGSLLMS RDDVRMSVEY LGPGDDASRD LSWLDWSSLD
     ALSADGRTLA IDESGEGSAG ETATYIRKSD GSPAVRIGAR WTGHALSPDG KSLLSTDDLT
     PNATGFWLVP LRAGAPVHVE NGLEFNRGIA AWFPDSKRIV YTANERGHEP RVYVQDVGGA
     ARALTPEGDQ FVALSPDAAE VLVRSAKGYS IYPASGGNPR PASVLTPQDT VLGFADGGKS
     VYLVTAQERN RIFRVDLSGG RRELWKELHP PDPAGMRGVG QIKITADGKS IASSVNRTLS
     ELYLVHIAK
//