ID   PKN1_CALS4              Reviewed;         625 AA.
AC   Q8R9T6;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable serine/threonine-protein kinase Sps1;
DE            EC=2.7.11.1;
GN   Name=sps1; OrderedLocusNames=TTE1500;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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   -!- 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;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AE008691; AAM24718.1; -; Genomic_DNA.
DR   RefSeq; WP_009611132.1; NC_003869.1.
DR   AlphaFoldDB; Q8R9T6; -.
DR   SMR; Q8R9T6; -.
DR   STRING; 273068.TTE1500; -.
DR   PRIDE; Q8R9T6; -.
DR   EnsemblBacteria; AAM24718; AAM24718; TTE1500.
DR   KEGG; tte:TTE1500; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_9; -.
DR   OMA; DPDYRYQ; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000000555; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..625
FT                   /note="Probable serine/threonine-protein kinase Sps1"
FT                   /id="PRO_0000171246"
FT   DOMAIN          10..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          344..410
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          411..477
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          478..545
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   625 AA;  69850 MW;  2F10C267A028347E CRC64;
     MIGRMLGNRY EILEKIGEGG MAKVYKAKCH LLNRIVAIKI LRPEFAADEN FVKKFKRESQ
     AAASLSHPNI VGIYDVGQEG DIYYIVMEYV KGRTLKELIR ENGGPLEVKR AVEIASQVCR
     ALDHAHKNKI IHRDIKPQNI LVTDEDVVKV TDFGIARAAN GATITYTGDV IGTAYYFSPE
     QAKGSIVDER TDIYSLGIVL FEMLTGKVPF EGDSPISVAL KHIQEDILPP SRLNEKVPEE
     LDKIVLKATQ KDPNLRYQTA SEFLKDLDTF LKNPKDLKFE EKDFEKTKVM PSREAEELKR
     AALKREREKK RKEIRKKVGI VLLVLLLLAS LSYGTVYVLN NFFKVNDVVV PNVVGLSLSQ
     ASKVLSEHNL KMEISEERYS DKPENTILEQ DPPQGALVKP GTTVYVVISK GRQMVIVPNV
     IGRDYLEAKN VLENAGLKVN IIENYNEQYQ KGYVFDQNPR YGVQVEYGTT IDVYVSKGPK
     PSIVPNVVNM NLDEAKASLE SAGLTLGKVI YKEADNVPEN TVLEQSVPPD TEVQKGSPID
     LIVSKLPQNS LQQQTKNVII NLPNKDGPMK VEVYVIQDGQ KNLVYSGEHT SSDSPLTVPV
     TAHKGKAVIE VDIDGQVYSR VEARF