ID   Q02A04_SOLUE            Unreviewed;       817 AA.
AC   Q02A04;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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_1128 {ECO:0000313|EMBL:ABJ82122.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ82122.1};
RN   [1] {ECO:0000313|EMBL:ABJ82122.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ82122.1};
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; ABJ82122.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q02A04; -.
DR   STRING; 234267.Acid_1128; -.
DR   KEGG; sus:Acid_1128; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_007799_0_0_0; -.
DR   InParanoid; Q02A04; -.
DR   OrthoDB; 9801841at2; -.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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   Pfam; PF13374; TPR_10; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-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:ABJ82122.1};
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:ABJ82122.1};
KW   Transferase {ECO:0000313|EMBL:ABJ82122.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        375..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..350
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   817 AA;  89175 MW;  097902D5B9677BB0 CRC64;
     MTGARWSEVK AVLSSVLETD PAGRAVRLGE LCGGDAELRA SVEALVALET RAGDLLNTGA
     APGAALRAGE AAPEAIGPYR VLRQIGRGGM GVVYLGARAD GEYQKQVAIK LITSGWRDAG
     LERRFRRERQ ILAQLDHPGI ARLLDGGSTA DGQPYFVMEY IEGLGLLEYC ARHELDIKQR
     LTLFLAVCDA VGYAHQRLIV HRDLKPGNIL VTTEGAPRLL DFGLARVLER DAASEEATQG
     IPLMTPAYAS PEQVRGEPDA VPGDVYSLGV ILYELLAGRR PYEVKTGSLL EMARAICEQE
     PAPLSQGASG SLARRLVGDL ENIAAKALAK DACRRYPSVG ELAADLRRHL EGRPVHARTA
     TFGYRVGKAL RRHRVAIPAA ALAAVLVLGF AGATWWEARR AERRFQQVRS LASSVMFELH
     DSIQRLPGSI TARELLVRRA LEYLESLSRE AGDRPDLQRD VALGYARIAE VEGFMGESNL
     GRVQASLASY RKAEAMLDRL VRRTPADPRL RHEYNEVANR LAGQLSSTGD LNSAKELTRK
     NVAFAEASVQ ADQGNTTALG DLSATLSALA DLYADQQRYA DAIPVRQRVE QLTAKLAELR
     PESDETRRNL ALARKRLGAL YGVMKRYEEC RAEYEQARAI DEQRAAASPM ESRAALDLSY
     DYSDLGWVAA RMQHYPEALS AHRRALALRT AAAQADPKDR RAASAVASST NRIGALLHKM
     GDLPGSLEML GRALALREEL VKRAASDWQA ARELADAHID IAETLADMKN PARAIAEFER
     GRAIYGELSA RGVLGPADAR FMREVEAEEA KVRLVAR
//