ID   PKNA_NOSS1              Reviewed;         564 AA.
AC   P54734;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Serine/threonine-protein kinase PknA;
DE            EC=2.7.11.1;
GN   Name=pknA; OrderedLocusNames=alr4366;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7505448; DOI=10.1073/pnas.90.24.11840;
RA   Zhang C.C.;
RT   "A gene encoding a protein related to eukaryotic protein kinases from the
RT   filamentous heterocystous cyanobacterium Anabaena PCC 7120.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11840-11844(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Probably required for both normal cellular growth and
CC       differentiation. Inactivation of pknA leads to colonies that appear
CC       light green and rough in the absence of combined nitrogen.
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; U00484; AAB41116.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB76065.1; -; Genomic_DNA.
DR   PIR; AF2351; AF2351.
DR   RefSeq; WP_010998503.1; NZ_RSCN01000027.1.
DR   AlphaFoldDB; P54734; -.
DR   SMR; P54734; -.
DR   STRING; 103690.17133502; -.
DR   EnsemblBacteria; BAB76065; BAB76065; BAB76065.
DR   KEGG; ana:alr4366; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   OMA; YLCEHSV; -.
DR   OrthoDB; 1377603at2; -.
DR   BRENDA; 2.7.11.1; 319.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; SSF54427; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..564
FT                   /note="Serine/threonine-protein kinase PknA"
FT                   /id="PRO_0000171181"
FT   DOMAIN          9..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          360..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        265
FT                   /note="E -> Q (in Ref. 1; AAB41116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        522
FT                   /note="A -> R (in Ref. 1; AAB41116)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  62385 MW;  AD0485E7AC69E785 CRC64;
     MEQLLDNRYR VIKTLGSGGF GETFLAEDSQ MPSNRRCVVK QLRPIHNNPQ IYQLVQERFQ
     REAAILEDLG SYSGQIPTLY AYFQSNTQFY VVQEWVEGDT LTAKLKQQGV LSESAVRDIL
     INLLPVLEYV HSKRIIHRDI KPDNIILRHR DGKPVLIDFG AVRESMGTVI NSQGNPTSSI
     VIGTPGYMPS EQAAGRPVYS SDLYSLGLTA IYLLTGKQPQ ELETEPHSGE IIWHRYALNI
     SPTLAAVIDR AIAYHPRERF TTAREMLEAL QLGVVSYPPT VPYQQPQSSP TVPYQQPPVV
     TTPPFATQTN TVAVSPGTAP TPQPINHNNS NKGILMGSLI AGGLIGASVV IGFALTRPNQ
     PVTQTTSLPS ETTISNNDTP TVEPSPTDTP ETPISQTVTQ DPTPQASVRF PINSRPFTTP
     IDSKPRNTTE PTTSVPQPTT PSEPQITTPV EATDRPSPEQ AVQNYYETIN QGEYSTAWNL
     LASSFQNNRK LHPRGYDSYL DWWGGQVENV DVEQVSLLKA NADTATVNAR LRYFMKSGRQ
     SSSSVRFSLV WDADNNRWVV SGAR