ID Q7UJC1_RHOBA Unreviewed; 880 AA. AC Q7UJC1; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 118. 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=RB11988 {ECO:0000313|EMBL:CAD77337.1}; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD77337.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD77337.1, 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; BX294154; CAD77337.1; -; Genomic_DNA. DR RefSeq; NP_870262.1; NC_005027.1. DR RefSeq; WP_011123523.1; NC_005027.1. DR AlphaFoldDB; Q7UJC1; -. DR STRING; 243090.RB11988; -. DR EnsemblBacteria; CAD77337; CAD77337; RB11988. DR KEGG; rba:RB11988; -. DR PATRIC; fig|243090.15.peg.5794; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_327020_0_0_0; -. DR InParanoid; Q7UJC1; -. 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:CAD77337.1}; 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 Transferase {ECO:0000313|EMBL:CAD77337.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167..187 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 585..860 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 59..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 95..152 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..114 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..145 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 614 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 880 AA; 97922 MW; 34FCCED377C4A0DC CRC64; MMDADRYQRV RDLFWEAEEI EEVAREKFIR DQAAGDEELI REVLSLLAEH DPNAARVEGA ATRPRPGNGS VPFGQGLPTP RETTESEVIR AIRSMSETAS DAKPESNGET VPGSIPGNAS AGHTVHAAQR THAMPRHDAN RPQPSRSRQR KTLTSIGPIN RAKQYNWVVW LLTAVTITCI WVVAAWVDRR LQRQADLSIQ RSLSLALDLS TIKVEQLLNR DKQFAIDLAR QPEVRNAIRS RSKNLSSAEL ADSIENQTLL FTQAVRNVNA DRPEFESHDL PAFQPPDVIF FSRDLQPLTI VFGNDRGRSM TDEANVQLPP DGAADLARAL SGRTVLHAPS PLATLLGKTL ADELDHAVSN PLAWIVPVHE QSSAETEEPD SLRSDVLGAA VIIPPNTSRW LNETLALISH ANSVDAYLVD RDGFMQTRSL NLPEQITQSL GARFRVTEIA NPSEAEERLN QLVAQLDRLT ESAMLNPNSE SSIGRTIHPL TIAAASVSHS PEPQVHGQTY RTYTGKDCVG VWQWLPEFGM GLIIESDSHQ LTYPLASTWP WALLLSIASI LPILVAKRLL KGPAPSALKQ PLGRYHIHEE LGAGGMGVVY RASHTELGRE IALKVLRVDR QDDDDHRRFD REARLAASLC SPHSVTIYDY GHNEHGEAFC VMQLLDGLTL SEIVARSGHQ EPARAIWIMR QVCQAVLEAH SQGLMHRDLK PQNIMLSFDT IVGDWAVVFD FGLAKPLEPN QGVFQTAETV WAGTPMYMAP ERFRAPSVMD PRSDVYSLGC VLYFLLSGRP PFAECDPESM FALILTQQPL EIETHRGEPV EAELNALVQA CMAKDKHDRV GSVADLIQRL DALAPRYPWT QEDARHWWQR HADEELAKKL //