ID   PKNB_BIFLO              Reviewed;         690 AA.
AC   Q8G6P9;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable serine/threonine-protein kinase PknB;
DE            EC=2.7.11.1;
GN   Name=pknB; OrderedLocusNames=BL0589;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN24413.1; -; Genomic_DNA.
DR   RefSeq; NP_695777.1; NC_004307.2.
DR   RefSeq; WP_011068568.1; NC_004307.2.
DR   AlphaFoldDB; Q8G6P9; -.
DR   SMR; Q8G6P9; -.
DR   STRING; 206672.BL0589; -.
DR   PRIDE; Q8G6P9; -.
DR   EnsemblBacteria; AAN24413; AAN24413; BL0589.
DR   KEGG; blo:BL0589; -.
DR   PATRIC; fig|206672.9.peg.1329; -.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OMA; DPDYRYQ; -.
DR   PhylomeDB; Q8G6P9; -.
DR   Proteomes; UP000000439; 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; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51178; PASTA; 4.
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..690
FT                   /note="Probable serine/threonine-protein kinase PknB"
FT                   /id="PRO_0000171185"
FT   DOMAIN          14..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          399..467
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          468..536
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          540..601
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          602..666
FT                   /note="PASTA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          429..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   690 AA;  72244 MW;  6A419EA8CED5D92D CRC64;
     MSTSMPTALA GGRYQLGQLI GRGGMAEVHV ALDTRLGRTV AVKIMRADLA NDDIFLARFR
     REAHAVAQMN NPNIVNIYDS GEELVSSESG DAERLPYIVM EYVKGQTLRD IIKVNGALSQ
     RDCEQVMLGV LNALDYSHRM GIIHRDIKPG NIMISEQGVV KVMDFGIARA LDDSAATMTQ
     SQGVVGTAQY LSPEQARGET VDMRSDLYSA GCVLYEMLTG RPPFTGDSAV AIAYQHVSEV
     ATPPSAAVPG LPKMWDSICA KAMAKDRQNR YATASEFKTD ILTYMNGGVP VAAAFNPLTD
     LSNMKARKEA ERDLPTTPVE PHQQPTQAFN PVTGQFEQIP PANGANAAAL QSRAQQRAAA
     AKAKKRKKII IGSVIAAIVA VLVIVGIVFA MNGSGNKSSE DTVTIPEVCN ASTSKDNIKL
     KLEASGLKMT EKQDTDSTEP EGTCTKMSPD AGSKVAKGSA VKVWFSAGPQ STQVPDVKER
     SQEEARSILE SAGFKVNAAV KTEDSADIAK DMVTKTDPAA GQSVPKGTTI TIYVSSGMTT
     VPSNLVGQSK DSVLQQYEGK FSFTVEQESS DTVEAGLITR VSPDSGSSIA QGGFITIWVS
     TGKEKVAVPN ITAGTDYVTA ELMLKAVGLK AQANGPTGST AVVVSINPGA GSQVDAGSTV
     TITTKAGSTG GGTGTGDGGN GTGNGGGTGE