ID   PKNA2_BIFLO             Reviewed;         757 AA.
AC   Q8G4G1;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Probable serine/threonine-protein kinase pknA2;
DE            EC=2.7.11.1;
GN   Name=pknA2; OrderedLocusNames=BL1425;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; 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; AAN25222.1; -; Genomic_DNA.
DR   RefSeq; NP_696586.1; NC_004307.2.
DR   RefSeq; WP_011068042.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4G1; -.
DR   SMR; Q8G4G1; -.
DR   STRING; 206672.BL1425; -.
DR   EnsemblBacteria; AAN25222; AAN25222; BL1425.
DR   KEGG; blo:BL1425; -.
DR   PATRIC; fig|206672.9.peg.283; -.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OrthoDB; 9762169at2; -.
DR   PhylomeDB; Q8G4G1; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
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..757
FT                   /note="Probable serine/threonine-protein kinase pknA2"
FT                   /id="PRO_0000171184"
FT   DOMAIN          14..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          466..539
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          545..614
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          615..681
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          344..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
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   757 AA;  80088 MW;  D7916F1B880268D1 CRC64;
     MSENEPAQMI EGRYRIVRNI AEGGMATVYE AIDERLGRTV AIKVMHTQLA KGPHREQFVE
     RFRREANSAA SIANPHIVQV YDTGEFNGLD FLVMEYVHGV NLRHEMNAQG TFSVRETLRV
     VAETLDGLAS AHRAGVVHRD IKPENILIND RGHVQITDFG LAKAASQATL SSTGMLLGTA
     AYLAPEMIEN NQATAQGDLY SVGIMAWEML TGKVPFDSDN PVTLVFKHVH EDVPSVATVC
     QGIDPSVAAF IAHLTARQVD ARPTDGAAAA EELSQLAAKL PLEAWQYRLH AEPIGGDHTD
     ATAAALVGNI AEQAPLTGVP AGAATFKPSV PAFLADDVAS NTVDTGGAAD VNPPAPPVAP
     TTALDSSTPA DASAPHKTQI MAQSGSETQV LPQAGDAFTR ALAFSDEPDV ASNGTGPKKQ
     RSKKPLIIVL VIVLVLAAIG GTAGWWWFAG PGSYWSVPKP DDVTCDANAS TECSLAGADW
     ATYESTLKAL GIPYKTHKEY SDDVAEGKII SSSVNKTKAV VNSRISKRAN QELTVVVSKG
     VRMTTIPKDI LDANSANGKD PLNALKKAGF DNVKHDESKD EYSMDTPQGV ALTISPDPGT
     TAKHNDEVTV TLSKGPMPVT MPNIVGKTQD EMQAALGELK LTANVTEQYD DKVEAGQVIS
     ASQEAGAQLK WGDSVDVVIS KGPEMATIPS GLVGKQESAV TKTLEGLGFE VKTDKVLGGL
     FGTVRTVKSG DTDLSNGGKI RLRDANGNPT VITLTIV
//