ID   PKN1_MYXXA              Reviewed;         693 AA.
AC   P33973;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Serine/threonine-protein kinase Pkn1;
DE            EC=2.7.11.1;
GN   Name=pkn1;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DZF1;
RX   PubMed=1835671; DOI=10.1016/0092-8674(91)90372-6;
RA   Munoz-Dorado J., Inouye S., Inouye M.;
RT   "A gene encoding a protein serine/threonine kinase is required for normal
RT   development of M. xanthus, a Gram-negative bacterium.";
RL   Cell 67:995-1006(1991).
CC   -!- FUNCTION: Plays an essential role in proper timing of early development
CC       events.
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   -!- ACTIVITY REGULATION: May be regulated by calcium or a calmodulin-like
CC       protein.
CC   -!- DEVELOPMENTAL STAGE: Developmentally regulated to start immediately
CC       before spore formation.
CC   -!- PTM: Autophosphorylated.
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; M73498; AAA25402.1; -; Genomic_DNA.
DR   PIR; A41090; A41090.
DR   AlphaFoldDB; P33973; -.
DR   SMR; P33973; -.
DR   BRENDA; 2.7.11.10; 3551.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
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; IPR009875; PilZ_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF07238; PilZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; TPR repeat; Transferase.
FT   CHAIN           1..693
FT                   /note="Serine/threonine-protein kinase Pkn1"
FT                   /id="PRO_0000171227"
FT   DOMAIN          59..328
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          393..491
FT                   /note="PilZ"
FT   REPEAT          630..663
FT                   /note="TPR"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         65..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         88
FT                   /note="K->N: Loss of ATP-binding."
SQ   SEQUENCE   693 AA;  74173 MW;  ED532EABF7215A91 CRC64;
     MPEVSSGGGC GACGRRHGAD ASCPTLVRAD VRAGGTAHPR CAPVVEAQDP LVGVRCGSFR
     LVRRLGRGGM GAVYLGEHVS IGSRVAVKVL HAHLTMYPEL VQRFHAEARA VNLIGHENIV
     SIFDMDATPP RPYLIMEFLD GAPLSAWVGT PLAAGAVVSV LSQVCDALQA AHARGIVHRD
     LKPDNIFLVR RNGNAPFVKV LDFGIAKLAD AHMPQTHAGI IVGTPEYMAP EQSLGRGVDG
     RADLYALGVI AYQLLTGRLP FNDEGLAAQL VAHQLRPPPP PSSVYPAVSA ALEHVILRAL
     AKKPEDRYAS IAAFRNALQV ALAEHVRVSA RKTRPGGLAV LERAPVAPDM PTEGQSRGRL
     GVDARAGHVP SSLASTSQRR LAPAAPAVPR ASLVEVPVQV VLRPGESPVR LRGSGLSRGG
     LFLHGGRVLP PLCSRLPVVL ELASGPLSVM CEVVRVVPPA QARVWGMPTG FGVQFVEATA
     VLKAAVDALL QGEPVRAVPQ VPLTEDPAVA RLLEAWRQRS AGDAYAVLAL EPDSDMGTVR
     LRTREAWRSL ESLEQHSLTP PQRAQVDALR VRVREAAEAL GATVQRALYD AWRGNHRGVA
     KCLEAGLTAE QLESLRREFL ARRPQAMGTA RSHFQSGGAL ERDGQLSQAL DQYERGLKLA
     PLEVDMLQRY RRLRRVLGGR ATAPTGHDRA RSP