ID Q04FQ7_OENOB Unreviewed; 614 AA. AC Q04FQ7; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, 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 OrderedLocusNames=OEOE_0789 {ECO:0000313|EMBL:ABJ56715.1}; OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Oenococcus. OX NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ56715.1, ECO:0000313|Proteomes:UP000000774}; RN [1] {ECO:0000313|EMBL:ABJ56715.1, ECO:0000313|Proteomes:UP000000774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P., RA Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). 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; CP000411; ABJ56715.1; -; Genomic_DNA. DR RefSeq; WP_002818671.1; NC_008528.1. DR AlphaFoldDB; Q04FQ7; -. DR STRING; 203123.OEOE_0789; -. DR GeneID; 75066136; -. DR KEGG; ooe:OEOE_0789; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR Proteomes; UP000000774; 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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABJ56715.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000774}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ56715.1}; KW Transferase {ECO:0000313|EMBL:ABJ56715.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 342..364 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 11..271 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 364..431 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 432..499 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 500..564 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 312..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 566..614 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 614 AA; 66659 MW; D89BDAAC523A2C30 CRC64; MNPGSTFANR YRIIRPLGEG GMANVYLAVD TKNNQQVAIK VLRLDLQNNP DFVRRFQREA QAAAQLLHPN IVKVLDAGSF DGVQYLTMEY VDGMDLKKYI SQYYPVPYAQ VVNIMEQVLS AVSMAHNHGI VHRDLKPQNI LVGKDGSIKI VDFGIAIARS EFGMTQTNAV LGSVHYLSPE QTRGGMATNK SDIYALGVIL FEMLTGQVPY KGETVVSIAM KHSSEQMPSA KDIDPNIPQA LENVILRATA KNPDNRYLTA EDMANDLRTS LSPRRANEAK LPPFTDDQAE TRTIPIDDLK SQVASGIQRL DPVYTPLKDN PDSTSDSKKV VPGKKKKRKH KIWPWILAGL LAIGFGVILV AMFWPGRVQV PDTANYKLSV AEKLIRENDL EVGSISETTS RKVKKGRVIK SDPKIGSHVA KNTKIDLIVS NGAKKLTFGD YVGSNYSDVA SVLRNQGYKV KKVEKYSNSV SSGQIIKQSV DADKKVDPYE TTVKFTVSKG AQKITVPTFD SLSEAQSWAD QNGITLKIAY SQSSDTDTGY VISQNPNGGT EISSSTVVHI LVAQRVDNSS SSSSSAVPSS SSSMSSSSNG SSSSSSNSSS SSSSSISSSS SPQK //