ID Q7UQX0_RHOBA Unreviewed; 769 AA. AC Q7UQX0; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 128. 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=RB6033 {ECO:0000313|EMBL:CAD74574.1}; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD74574.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD74574.1, 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; BX294143; CAD74574.1; -; Genomic_DNA. DR RefSeq; NP_867032.1; NC_005027.1. DR RefSeq; WP_011120731.1; NC_005027.1. DR AlphaFoldDB; Q7UQX0; -. DR STRING; 243090.RB6033; -. DR EnsemblBacteria; CAD74574; CAD74574; RB6033. DR KEGG; rba:RB6033; -. DR PATRIC; fig|243090.15.peg.2911; -. DR eggNOG; COG0457; Bacteria. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_363256_0_0_0; -. DR InParanoid; Q7UQX0; -. 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; 1.25.40.10; Tetratricopeptide repeat domain; 2. 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 InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48452; TPR-like; 2. 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}; Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000313|EMBL:CAD74574.1}; 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:CAD74574.1}; KW Transferase {ECO:0000313|EMBL:CAD74574.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 366..386 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 87..346 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT COILED 574..601 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 769 AA; 85622 MW; 99E55E82B34D9E99 CRC64; MNADLDTTDE RLLSVLEEYL ERRSAGSVTH HDFIAECQER YSDGRFEDRL PGLLTSLDAL HGFAPESESA SPAPVWGGLA SRTIGDFEVI REIGRGGMGI VYEAKQLSLE RIVALKILPR SITLDQKQVA RFIFEAQAAG GLHHPNIVPI YGAGIEDGIH CYSMPLIRGR SLDEFIYTDR PEVEDAIRWA LQVANAIDHA HRYGVIHRDI KPSNLIVDQD GKIWVTDFGL ARCRQGNGSD VNGITGSNAV VGTLRYMSPE QSLGKASFVD HRADVYSLGV TLYEMLCGER FDGSDPASVR RRNPKVSRDL ETVLIKSLAK EPAERYSAAG DLAEDLRRVS DGLPILARRP SLSDRVTKWT VRHRRVVAST AAAVLVALVL SLMAMLKFVQ QRSALRSALA QSDSSLVMAA RNYEKAQANF QQTREVLDHF GLMAAERLRG VAGAESVRED LVGALLQYYE RFAGEVEAAP ELRNELARTH LRAAKIIEEI GATRRALATY QRAATILLEL PPLPANEHEL ALCLNSIAVL QAEHGETPQA ESNYQKAIQR LESLDRHETM AMVRGNYGLL LSSVNRQEDA KRELERAIDE LSRMESESQS TRLIAAKIWN NLSHLAQHGD LEGALGMNQK AIDLLRVGRR PDHDRGPSDG DRRDFEKKHA LAQSLSNQAA LLMRLGRHDD AVVCYQDSVA YLREIVEEMP MAVRYAEELA ITYNNLSRLL SQQSRMPEAL HATIQARNLM RSLVQRLPNE DRYQEALAGV QKNLEGFAP //