ID A0ZZD6_BIFAA Unreviewed; 686 AA. AC A0ZZD6; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 105. 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=pknB {ECO:0000313|EMBL:BAF38819.1}; GN OrderedLocusNames=BAD_0038 {ECO:0000313|EMBL:BAF38819.1}; 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:BAF38819.1, ECO:0000313|Proteomes:UP000008702}; RN [1] {ECO:0000313|EMBL:BAF38819.1, 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}; 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; AP009256; BAF38819.1; -; Genomic_DNA. DR RefSeq; WP_011742591.1; NC_008618.1. DR AlphaFoldDB; A0ZZD6; -. DR STRING; 367928.BAD_0038; -. DR PaxDb; 1680-BADO_0028; -. DR KEGG; bad:BAD_0038; -. 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: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; cd06577; PASTA_pknB; 4. 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; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF03793; PASTA; 4. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 4. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAF38819.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008702}; KW Transferase {ECO:0000313|EMBL:BAF38819.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 368..390 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 14..282 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 396..465 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 466..533 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 537..600 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 601..662 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 429..453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 636..686 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..453 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 686 AA; 72881 MW; EF052680581F6485 CRC64; MNINMPTSLA GGRYQLGQLV GRGGMAEVHV ATDTRLGRTV AVKIMRADFA TDSIFLERFR REAHSVAQMN NPNIVNIYDS GEETVTTETG EIEHLPYLVM EYVKGQTLRD ILKVNGALSQ RDAEQVMMGV LNALEYSHRM GIIHRDIKPG NIMISEQGVV KVMDFGIARA IDDSAATMTQ SQGVVGTAQY LSPEQARGES VDMRSDLYSA GCVLYEMLTG RPPFTGDSAV AIAYQHVSEV ATPPSTIVPG LPKMWDSICA KAMAKDRQNR YATASEFKND LLTFMNGGVP MAAAFNPLTD LTNMKARKQA EMDAATVPMA PATDAPTQAF NPVTGQFEAV PNPNGGVETK TRAEQRAKAV QERKKKQIII ASVVGSIVVL LAVIGIFFAL NGHKNTADLV SVPDFTDTSN ISQARVEEQL KALGLKLDAR DDATSSQPKG TITKQNPQGG RKVAKGSTVS VWFSTGPQAV PVPDVSGKTQ EEAKSILEAA GFKVGNVKTV DNATIAKDQV VNTDPAANSK QTKGTIITLY ISSGMTKIPD GLVGQAKDSV IAQLKQAGLT QITIESEYSD SVQSGAVTRI DPGSGSTVEM GTAVTIWVST GKQQTSVPNV AGMNYADAKA LLEGYGFQVN VSGPQDGTVA SMSPNGGSKA DNGSTITLTT KAQPATDTGD NSNGNTTDNN QQQPQH //