ID   Q02AP6_SOLUE            Unreviewed;       880 AA.
AC   Q02AP6;
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_0871 {ECO:0000313|EMBL:ABJ81870.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ81870.1};
RN   [1] {ECO:0000313|EMBL:ABJ81870.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ81870.1};
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; ABJ81870.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q02AP6; -.
DR   STRING; 234267.Acid_0871; -.
DR   KEGG; sus:Acid_0871; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_007799_0_0_0; -.
DR   InParanoid; Q02AP6; -.
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; 1.
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   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; 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:ABJ81870.1};
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:ABJ81870.1};
KW   Transferase {ECO:0000313|EMBL:ABJ81870.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        354..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..331
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   880 AA;  96973 MW;  0CBE81F97754EE86 CRC64;
     MNRQVEILVD QAAQLPQESR AAFLDRACPD PRLRAEVAAL VQFAAEAESF FDHAIQGVAS
     ALRSRHEPVP GDHIGSYRII SSIGLGGMGS VYLAERADGE IQQRVAIKLL RADGHRPEWR
     ERFLKERQLL ASLNHPSVVH VIDAGHTQDG RPFLVMEHVE GLPIDQYAAG IAVANRLKLF
     VRVCDAVSHA HRHLIIHRDL KPQNILVDST GQPKLLDFGI AKLVNETGDA TENAEQLLTP
     NYASPEQFRG EAQSTATDVY SLGAVLYKLL TGSAPREHAR TGAMPEPAAP SRLNGDVPRD
     VDFVVAKALR PEPEHRYASV DEFANDVRAV LERRPVQARE GDRAYRVGRY LTRYWIPVAA
     ALLIVASLAA GLLIANRERR LAERRFADVR QLATKLFDID VQVAQLPGGS RTRQLIVDTA
     LEYLKRVTED VRMDPTLALE LGTAYMRVAR VQGVNISPNL GQTERAERTA RNAQALIDSV
     LEREPKNRIA LLRAGQIAHD RMILAGDAQN ADQALQFART SIERLNQYLA TGPLSASSDR
     MEAQQVILAL INVANRFLKA DQFEDALQTA GRAIEIARVT NWPTQAGAAL IVVALAQRDQ
     GDLDNALKSV RESIRLLEPE PGEKAAGRLQ AYGLALMREG QILGEDQAIS LNQPQAALKS
     IQRALEIGED FARRDRSDFQ SQYRVYSAET KMAAILRHTD PARALAMYDD GLRRLALTAA
     NAGTVRNEIA TLAASARILL RLGRRAEARR RLDAAFVRLG RLNLYPAPRI ELGTPAADAL
     RAQAAYEAAA DAGRGAALYE ELLRLILAAH PKPETSLEDA LDLSNIYADV AAAHRRAKQS
     DLAAGVEARR LSLWQLWDHK LPNNSFVQSQ LESARRASYN
//