ID Q8G6I0_BIFLO Unreviewed; 746 AA. AC Q8G6I0; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 130. DE SubName: Full=Widely conserved protein with eukaryotic protein kinase domain {ECO:0000313|EMBL:AAN24482.1}; GN OrderedLocusNames=BL0660 {ECO:0000313|EMBL:AAN24482.1}; OS Bifidobacterium longum (strain NCC 2705). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24482.1, ECO:0000313|Proteomes:UP000000439}; RN [1] {ECO:0000313|EMBL:AAN24482.1, ECO:0000313|Proteomes:UP000000439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439}; 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 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014295; AAN24482.1; -; Genomic_DNA. DR RefSeq; NP_695846.1; NC_004307.2. DR AlphaFoldDB; Q8G6I0; -. DR STRING; 206672.BL0660; -. DR EnsemblBacteria; AAN24482; AAN24482; BL0660. DR KEGG; blo:BL0660; -. DR PATRIC; fig|206672.9.peg.1391; -. DR HOGENOM; CLU_000288_135_6_11; -. DR OrthoDB; 9762169at2; -. DR Proteomes; UP000000439; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AAN24482.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000439}; KW Transferase {ECO:0000313|EMBL:AAN24482.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 542..562 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 603..628 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 648..669 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 718..740 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 28..298 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 68..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 447..476 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 458..473 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 746 AA; 77844 MW; 4A62BA752E69A034 CRC64; MHQQGIRMEG MSDLNALNLE SGEVVGGYTL ISRLGSGAMG SVWRVRDDGG TTYAMKILRD SLTDESVAGS GSASTALHDP DLKPDVTPRE RLRREAMALK KVNHPGVCGI VDMELDDTLA FIVTELIEGK NLKDDVAANG RYVGDDLERL ARKLIEATKA VHAAGIVHRD IKPTNVMVSA AGPVLVDFGI AMGEGESHVT RTGLVMGTPG FIAPEIIDGA ESDDATDWWS VASVLAFAAT GAPVFGTKPM MAVLEREASG NANLSGLPAG TLAAFRSALD PDRRDRCTPD QLLNAIALDA LNPNAWQGEQ AGPFAAGAVA GQPAAIVAEA AEAMPPFGAA GGVDRNNPRT IWRAAEEAAE APTMAVFSGN KGDNGDGETV VFSPAGAATA TLPLADMPPR PPAGAEQATQ LLPDAAADFT DDAGTQVLTG ATTPMPDQTT PLAERTTVLP TPQPSSFPPS GTAQSSWDPA SNQPTAVDPA IRPALQRIID QTAQAAPTET MVQNPPMPNP VDVKRGEYLQ RGTLPLILLA APLAALAANA PLVAIIAATA LLWLLLTLAY NTEPQLEREG KRGGERKNSD SWIRVATFPW HLVKALLLAI PRILLLVIIY MAGTAVATAA LALPVHTISW YFTADWGIPV PLLNDVPFSA SGLALGGFMA IGWLVTVFVP QSMMIRLGGG VLRGLKHSRP AGAPSTEVGG APPAPVAPAP KGGGRGTVLF TIWAIITVAL CAMPILGMPI NWMPFA //