ID Q7UJX4_RHOBA Unreviewed; 781 AA. AC Q7UJX4; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 124. 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=RB10995 {ECO:0000313|EMBL:CAD77107.1}; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD77107.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD77107.1, ECO:0000313|Proteomes:UP000001025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10527 / NCIMB 13988 / SH1 RC {ECO:0000313|Proteomes:UP000001025}; RX PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., RA Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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; BX294152; CAD77107.1; -; Genomic_DNA. DR RefSeq; NP_869729.1; NC_005027.1. DR RefSeq; WP_011123036.1; NC_005027.1. DR AlphaFoldDB; Q7UJX4; -. DR STRING; 243090.RB10995; -. DR EnsemblBacteria; CAD77107; CAD77107; RB10995. DR KEGG; rba:RB10995; -. DR PATRIC; fig|243090.15.peg.5315; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_358578_0_0_0; -. DR InParanoid; Q7UJX4; -. DR OrthoDB; 6111975at2; -. DR Proteomes; UP000001025; 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 CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:CAD77107.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001025}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAD77107.1}; KW Transferase {ECO:0000313|EMBL:CAD77107.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 414..438 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 89..389 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 184..219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..750 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 648..678 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 688..704 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 717..731 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 781 AA; 86534 MW; C239B866F9CEB883 CRC64; MNDGENMATF DETNDNGVVA AVKDYMRLLE NGKAPSIEDF LAGYASIEEE LRPALEGLAM LHGAGSPSEP STTAVGPDAE FTAKPIGDFQ IVGELGRGGM GVVYEAVQLS LGRKVALKVL PFASGLDEVR LQRFRNEAHA AAALHHTNIV PVYAVGSDRG VHYYAMQLID GRTLADVIDE MRQEAKNGKS NDTRPMRDSI SAAPTRSNNT TSMGTSMGRR RHYESAVRMA HEAAIAIEHA HQYGVIHRDI KPGNLLIDGA GKVWVTDFGL AHIESDTNNL TRTGDPMGTL RYASPEQASG NRMILDHRTD VYSFGVTLYE LLTLRPAIEG EGFRELLNAV IEVEPPSPMS IAPDLPTELD TIVRKAIAKQ PSERYATMKA LADDLQCWLD DKPIQAKPPT ALERLAKWRR RNSGLVAAAF GMLLIASVAL LVTALLVWRE QRQTQLALDR ETQQRELAEE SFQQARAAVD AFSELSESEL AYRAGLQDVR RTFLETSLSF YRDFLELRAD DPALKSELAK TSARVEAMVE ELQLLENIGP LLQLLEESVQ KELQIDREKA DAITDAVKML QSERHSLANE NPGNLSIENA DMTALLESFD SFLKQKLSPQ QVERLQQIAR QRRLPFTFKS AEVVAALEMT REQRVRIDQI IEETRPSRRG GFEGDRGPRD RDNGRRGPGP DGFEFGMRGR FDGGRFDDGR SPDGNGSRGG RPPEFGRPPE MNGPPEFGGP PGRKGPSGFN GPPHDMWNSD GTRYTVEKIL EILTPEQRQK WNELIGEPFV Q //