ID Q8A433_BACTN Unreviewed; 454 AA. AC Q8A433; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 135. DE SubName: Full=Serine/threonine-protein kinase pknB {ECO:0000313|EMBL:AAO77877.1}; GN OrderedLocusNames=BT_2771 {ECO:0000313|EMBL:AAO77877.1}; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77877.1, ECO:0000313|Proteomes:UP000001414}; RN [1] {ECO:0000313|EMBL:AAO77877.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414}; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., RA Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). RN [2] {ECO:0000313|EMBL:AAO77877.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414}; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of its two RT dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). 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; AE015928; AAO77877.1; -; Genomic_DNA. DR RefSeq; NP_811683.1; NC_004663.1. DR RefSeq; WP_008761998.1; NZ_UYXG01000001.1. DR AlphaFoldDB; Q8A433; -. DR STRING; 226186.BT_2771; -. DR PaxDb; 226186-BT_2771; -. DR EnsemblBacteria; AAO77877; AAO77877; BT_2771. DR GeneID; 60923949; -. DR KEGG; bth:BT_2771; -. DR PATRIC; fig|226186.12.peg.2818; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG1716; Bacteria. DR HOGENOM; CLU_602255_0_0_10; -. DR InParanoid; Q8A433; -. DR OrthoDB; 9813021at2; -. DR Proteomes; UP000001414; 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; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00060; FHA; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000253; FHA_dom. 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 InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1. DR PANTHER; PTHR24345:SF94; SERINE_THREONINE-PROTEIN KINASE PLK4; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00240; FHA; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 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:AAO77877.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001414}; KW Transferase {ECO:0000313|EMBL:AAO77877.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 402..421 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 433..452 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 4..263 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 275..330 FT /note="FHA" FT /evidence="ECO:0000259|PROSITE:PS50006" FT BINDING 32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 454 AA; 50989 MW; DD82AC5C9998FA25 CRC64; MPEYELIKVI GQGGMGSVYE GRSGDGKRVA IKMMNSKATM NPEFKELFYI EAAALKKMRH PSVVGIVDNP FSDEHGNMYL PMEYVDGETI EHHVEMAGPY TEFTAKDLMG KILDAMAYIH RMGCIHRDIK PSNIMVRPDG SICIIDFGIA KDMKTSTGKT IGRIIGTDGY MSPEQAKGDS IDYRTDIYSL GCLLHYMLTG SHAIKKRSND YDTICSILND EFPRAKTFNP HLSDQTQEAI LKAVDKNMLR RFQTVMEFKS GLFRETVVDP NRVKVSVGRR ECDITIPSDY ISGHHLEIEY REERCTGSIH RYLLFTDSST NGTSVDGKYL RHGSIKIPFS FENPSPLPNV WLAGRSEYLL DWDEVIQKLR DKGGRTVIME EVVGDILPPT PPTPSVKEDK LGIGYGILSV VCPIVGWVLW AQWKKETPRR ARAAAICGWI GFVVGFIINI LSSI //