ID   A1A262_BIFAA            Unreviewed;       732 AA.
AC   A1A262;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknA2 {ECO:0000313|EMBL:BAF39795.1};
GN   OrderedLocusNames=BAD_1014 {ECO:0000313|EMBL:BAF39795.1};
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39795.1, ECO:0000313|Proteomes:UP000008702};
RN   [1] {ECO:0000313|EMBL:BAF39795.1, ECO:0000313|Proteomes:UP000008702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC   {ECO:0000313|Proteomes:UP000008702};
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; AP009256; BAF39795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1A262; -.
DR   STRING; 367928.BAD_1014; -.
DR   PaxDb; 1680-BADO_1066; -.
DR   KEGG; bad:BAD_1014; -.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   Proteomes; UP000008702; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; -; 4.
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; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAF39795.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008702};
KW   Transferase {ECO:0000313|EMBL:BAF39795.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        403..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..292
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          588..654
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          655..728
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          308..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  79096 MW;  9AEC9CC75AFD5E3C CRC64;
     MKKESYRLAM SEAQHAPEGQ VIEGRYRVVS RIADGGMATV YQAVDERLGR TVAIKIMHTQ
     LAQGPQRDQF VERFHREARS AAAIANPHIV QVYDTGEFDG LDFLVMEYVH GVNLRYEMNQ
     QVTFSVRETL RIVGETLDGL ASAHRAGVVH RDIKPENILL NDRGHVQITD FGLAKAVSQA
     TLSSTGMLLG TAAYLAPEMI QHNQATPQGD LYSVGIMAWE MLAGKVPFTA DNPVTLVFKH
     VHEDVPDITT ACPGINAGVA AFLARLTARA VEDRPQDASV AFDELQQLQS NLTIDDWQYR
     LSAVSPAAND AADTMPGDGT RQMPLPPAPP APPVRQNDDR TRQFNPENPN KTTVMPAQQA
     DPEATTRLAL EKNDVPANNV PASPSNGPVS GGQPKRSGKR APVIIAVVAA IVLACAGGGG
     YAWWYFRGPG SYWTMPQPAD LTCSDSEPCR ISNIKWNAYE ELLKFSNIEY EETEAFSDSV
     KAGNVISTDP ENVGSHVSKR HHQKVKVVVS KGIKQGTVPT DILDATSANG KDPINALKRA
     GFDNIEQTPA NDDAYSMDVP QGALLDLSVD PGATLPHNAK ITVTLSQGPK PVTMPDVVGK
     SKDEAQQTLD ALKLTVNWTE QFDDKIPQGQ VISASAKTGD ELHWGDSVNA VVSKGPETVT
     LPNYVGQKAA AAKAALEKLG FSVKISSQLT LDSSQDKKVA SQDPVGGTEV RLRQEDGTPN
     TVTLKMYSSL FD
//