ID Q9K9Z0_HALH5 Unreviewed; 664 AA. AC Q9K9Z0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 142. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAB06223.1}; GN OrderedLocusNames=BH2504 {ECO:0000313|EMBL:BAB06223.1}; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). OX NCBI_TaxID=272558 {ECO:0000313|EMBL:BAB06223.1, ECO:0000313|Proteomes:UP000001258}; RN [1] {ECO:0000313|EMBL:BAB06223.1, ECO:0000313|Proteomes:UP000001258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 RC {ECO:0000313|Proteomes:UP000001258}; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans RT and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}. 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; BA000004; BAB06223.1; -; Genomic_DNA. DR PIR; H83962; H83962. DR RefSeq; WP_010898655.1; NC_002570.2. DR AlphaFoldDB; Q9K9Z0; -. DR STRING; 272558.gene:10728402; -. DR KEGG; bha:BH2504; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000001258; 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-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; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43671:SF13; LD04361P; 1. DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAB06223.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001258}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAB06223.1}; KW Transferase {ECO:0000313|EMBL:BAB06223.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 340..366 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 10..270 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 367..432 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 433..499 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 500..565 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 563..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 566..592 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 664 AA; 73720 MW; E2FF225DCCC6EE52 CRC64; MIGKRISGRY EILETIGGGG MADVYKAMDV ILDRQVAVKV LQAQFSKDEQ FIKRFRREAQ AATSLAHQNV VSIYDVGEEE NLYYIVMEYV EGPTLKELIQ QRGPLPVDET IDIMSQMMAA ISHAHMNQIV HRDIKPHNIL IGEDGVVKVT DFGIARAMSS ATITHTNSVM GSVHYLSPEQ ARGGLVTFKS DIYSLGIVLF EMVTGQLPFS GDTAVSIALK HLQNDIPSPK EIQPSLPQSI ENVIVKATAK DPFYRYGSVS EMDEDLSTAL DPARVNERPY DQKEDDEEAT KAIPIIKDEQ LEQEDFEKTM EAPPIKKVEE PKAPAAEEKV KKPKKKRRKW LWAVLIVLFL LIGTGVTALA LMPSWFQVDD VDVPDVRESS FEEAEAELRS LGLEVEREDV EDDAPAEEVV SQHPRPGSVV KQGSTVRLFV STGPEEGQMI DVTGRTIEEA QRLLNDFADV RLEERETNDV SPGIVIEQTP EAGESVVPEE TTVTLIYSAT SDIVLENMQG MTENEAHGYL QENGLRTRFS YDYSSSVAEG RVISHSPASG ATVSEGDDVT IVVSRGPEPQ TDQGGGQQEQ PQQPQQPQTR SHLVNQPIEA SQEVQVRIVY RDATTGGQDR VFIDETISET KTYQIPLEAS ADQPGSFDLY INGEFVKSSR EYTY //