ID   Q5L0R9_GEOKA            Unreviewed;       656 AA.
AC   Q5L0R9;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=GK1176 {ECO:0000313|EMBL:BAD75461.1};
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD75461.1, ECO:0000313|Proteomes:UP000001172};
RN   [1] {ECO:0000313|EMBL:BAD75461.1, ECO:0000313|Proteomes:UP000001172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426 {ECO:0000313|EMBL:BAD75461.1,
RC   ECO:0000313|Proteomes:UP000001172};
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75461.1; -; Genomic_DNA.
DR   RefSeq; WP_011230676.1; NC_006510.1.
DR   AlphaFoldDB; Q5L0R9; -.
DR   STRING; 235909.GK1176; -.
DR   KEGG; gka:GK1176; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_9; -.
DR   Proteomes; UP000001172; Chromosome.
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; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.40.2560; -; 1.
DR   Gene3D; 3.30.10.20; -; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
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:BAD75461.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001172};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAD75461.1};
KW   Transferase {ECO:0000313|EMBL:BAD75461.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        334..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          361..428
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          429..496
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          497..563
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   656 AA;  73042 MW;  5BD49214150BC8E5 CRC64;
     MLIGKRLNDR YKIISLIGGG GMANVYLARD MILERDVAVK VLRLDFANDD QFIKRFRREA
     QAATSLNHEH IVSIYDVGEE EGVYYIVMEY VRGATLKQYI QQHAPLPVER ALGIMDQLTS
     AIAHAHENGI IHRDIKPQNI LLDEHGNVKV TDFGIAVAMS GTTITQTNSV LGSVHYLSPE
     QARGGIATEK SDIYSLGIVM FELVTGRLPF SGESAVSIVL KHLQAETPSP KAWNPDIPQS
     VENIILKATA KDPFYRYQSA REMNEDIRTA LDPRRRNEPK FTIPDDDEEA TKAIPMIKHA
     ESAALEQETL VYEEKTSEPV HTTGEPKPKR KRVWIAWLVA ALLFIGAAGI SAVTWIPDLI
     FPKEVTMPNV VNKNYDDAVE QLSSLGLEIK DTIDVEDDQI EEGKVVRTDP EAGMTVKKGA
     GVIIYKSIGK KKIEFPSFIG DDIAAAEEEL RAEGFTRITR SGRYSDKPEG TILDQYPYAG
     DEVVPDETEV MFTVSLGPEK VTVKDLTGYT EKSVRDYGAD QGLRIDVKYE YSDEVPEGLV
     ISQTPAANER VKKGETITVV ISRGPEPKPS KTVVKEIMIP YEPAMPGQMV EAQLYIQDAT
     HNMSTPYKTY RLTAPATEMV EFEIPYGETA YYRVIVNNVV KEEGSIPYPE NNGKKG
//