ID Q819U5_BACCR Unreviewed; 657 AA. AC Q819U5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 134. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AAP10782.1}; DE EC=2.7.11.1 {ECO:0000313|EMBL:AAP10782.1}; GN OrderedLocusNames=BC_3860 {ECO:0000313|EMBL:AAP10782.1}; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10782.1, ECO:0000313|Proteomes:UP000001417}; RN [1] {ECO:0000313|EMBL:AAP10782.1, ECO:0000313|Proteomes:UP000001417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417}; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). 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; AE016877; AAP10782.1; -; Genomic_DNA. DR RefSeq; NP_833581.1; NC_004722.1. DR RefSeq; WP_000904747.1; NZ_CP034551.1. DR AlphaFoldDB; Q819U5; -. DR KEGG; bce:BC3860; -. DR PATRIC; fig|226900.8.peg.3979; -. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro. DR CDD; cd06577; PASTA_pknB; 2. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.60.40.2560; -; 1. DR Gene3D; 3.30.10.20; -; 3. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045269; Atg1-like. 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; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1. DR PANTHER; PTHR24348:SF77; SERINE_THREONINE-PROTEIN KINASE DDB_G0271538-RELATED; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF21160; PrkC-like_PASTA-like; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AAP10782.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001417}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AAP10782.1}; KW Transferase {ECO:0000313|EMBL:AAP10782.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 341..364 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 11..282 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 365..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..566 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 657 AA; 73782 MW; 2F84F117B53B486F CRC64; MLIGKRLNDR YKLLKMIGGG GMANVYLAHD DILGRDVAVK ILRLDYSNNE EFIKRFHREA QSVTTLSHPN IVNMYDVGEE DGIYYLVMEY VPGQTLKQYI IERGMLPIGE ALDIMEQLTS AMAHAHHFEI VHRDIKPHNI LIRADGIIKV TDFGIATATS ATTITHTNSV LGSVHYLSPE QARGGIANKQ SDIYSLGIVM FELLTGRQPF SGESAVAIAL KHLQSEIPSP KRWNENIPQS VENIILKATA KDPFHRYQSA NAMKRDIETA LYPERINEQP FYIPEDMEAT KAIPIIQQEQ LFENVSDETI VLKGSKVEEP IRAEAAELDK KKKRSNKWLK VLISTFLFLA IGITLALTVI PGLFIPKDVK VPDVAGMKYT TAVNTLVEKG FEVTEPNIVY TDDVEVGDVI KTDPVAGRVV KENAKITIYQ SGGKKKSKMA NFTGQNFESV KAELEEKYKQ VTVNYIENDK PKGEIVEQIP TPDQMVIEAE QELKIWVSKG PYQIRPGDFS GWTENSVTGY LNERKLTSDI KREYSDTVEK GLVISQFPKP GTPLKEGDKV TIIISDGQKP KVTKTVKLDN ISIPYEPAVT GEKKPQTIEI YKEDMQQKMD RPVETRTITE SATISLEFVI QEGSKGHYKI VRDGVTIIDK EVPYPTQ //