ID   PKNB_LACLA              Reviewed;         627 AA.
AC   Q9CEF5;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable serine/threonine-protein kinase PknB;
DE            EC=2.7.11.1;
GN   Name=pknB; OrderedLocusNames=LL1887; ORFNames=L138452;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05985.1; -; Genomic_DNA.
DR   PIR; G86860; G86860.
DR   RefSeq; NP_268044.1; NC_002662.1.
DR   RefSeq; WP_003130801.1; NC_002662.1.
DR   AlphaFoldDB; Q9CEF5; -.
DR   SMR; Q9CEF5; -.
DR   STRING; 272623.L138452; -.
DR   PaxDb; Q9CEF5; -.
DR   EnsemblBacteria; AAK05985; AAK05985; L138452.
DR   KEGG; lla:L138452; -.
DR   PATRIC; fig|272623.7.peg.2021; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_9; -.
DR   OMA; DPDYRYQ; -.
DR   Proteomes; UP000002196; 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..627
FT                   /note="Probable serine/threonine-protein kinase PknB"
FT                   /id="PRO_0000171200"
FT   DOMAIN          12..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          361..428
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          430..502
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          503..574
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          304..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         18..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   627 AA;  67878 MW;  00B30B68C5C28A81 CRC64;
     MIQIGKIFAD RYRIIKEIGR GGMANVYQGE DTFLGDRLVA IKVLRSNFEN DDIAIARFQR
     EAFAMAELSH PNIVGISDVG EFESQQYIVM EFVDGMTLKQ YINQNAPLAN DEAIEIITEI
     LSAMDMAHSH GIIHRDLKPQ NVLVSSSGTV KVTDFGIAKA LSETSLTQTN TMFGSVHYLS
     PEQARGSNAT VQSDIYAIGI ILFELLTGQI PFDGDSAVAI ALKHFQESIP SIINLNPEVP
     QALENVVIKA TAKDIKNRYT DVEEMMTDVA TSTSLDRRGE EKLVFNKDHD ETKIMPANLI
     NPYDTKPLID KKEDNDSQTD EKAASSEVGN KNKKSKKGLI IGLIILLLVV GGATLAWVVS
     TPTNVKIPNV TNSTLSQAKS KIKDAKLKVG TVHKQQSSTI AEGKVIKTDP TSGTTVRSNS
     SVDIYVSTGN EDIIKMKDFV GEKIDEAMAT LLKDYGIDES QVTQTSVPSD SYPAGTIIKQ
     SPKKGSSFDT KGSEKITFEV SSGKQVEVPD YKPNGQYMTY SQYQAALKAA GFTNITLDPQ
     ATTNQQADGY VYSVYPNVGT SVDPTQEIVV TYSVYTAPSS SSTTSESTTT SETSSSTTSS
     TSSSTTSQPS TDNNNSSKES STTSSSS