ID Q7UT11_RHOBA Unreviewed; 1287 AA. AC Q7UT11; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=ppkA {ECO:0000313|EMBL:CAD73631.1}; GN OrderedLocusNames=RB4186 {ECO:0000313|EMBL:CAD73631.1}; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD73631.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD73631.1, 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; BX294140; CAD73631.1; -; Genomic_DNA. DR RefSeq; NP_865945.1; NC_005027.1. DR RefSeq; WP_011119761.1; NC_005027.1. DR STRING; 243090.RB4186; -. DR EnsemblBacteria; CAD73631; CAD73631; RB4186. DR KEGG; rba:RB4186; -. DR PATRIC; fig|243090.15.peg.1944; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG1672; Bacteria. DR HOGENOM; CLU_262539_0_0_0; -. DR InParanoid; Q7UT11; -. DR OrthoDB; 5476445at2; -. DR Proteomes; UP000001025; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR041664; AAA_16. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1. DR Pfam; PF13191; AAA_16; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:CAD73631.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001025}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAD73631.1}; KW Transferase {ECO:0000313|EMBL:CAD73631.1}. FT DOMAIN 54..338 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 18..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 263..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 18..35 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1287 AA; 145328 MW; 8F551409E59BC64F CRC64; MSQWEDYTGD EWMRPLASQD TRTKHILDRE TQGIKPRPRL QAPPFKAGDT WGEFTLDEWL GSGTHGWVFA ARENATEKPV ALKILAVEDD PGTTLAKTGF RRMAKLNHRN LMRLHGIHEH DKTVAFSMER IDGVNLTTAI RRWRNEPLDV ACEHITEMVR QIGSAIGWMH ARELVHRDLK PSNIMVTDDY KRFVVIDYDS AGMFQEHDAE SMRAYLIWTP MYVAPEVLVR QRHTPSSDVF SLGMVVLEAL RVFSAAQYRR EGSLKVESRP TDGSDESLGI RRDKSNEKQD RMLITNAVRG LHPSIPADLL ETLDEMLAPD EADRPMAMTL SRLGRPLETM QMTRITDVDS SRVREATQQI RHDELARIHR WSHLVLGGQV QRLHLSGDSG IGKSTLLDVA LSQLRSLSWA QVFVARCQQR DQKPLQAFSQ ISDEITMRFR GMDREPLQVD SVTVSVLTSI LPGLAEVLEV DRSQPLLQTS PTRPGGLEAA LKVCERLREY GPVFFVIDDV QWADRDTISV LDYLQSGSMN RPKAPELQGL GLITVSRTDG DRQITLPDET INLGPLPDET AIEMLMREAS KYELEIPEAH LKDLASQIDG LPYRLDACLE ELRPGGWLSD AIQKNGEESD SMTVPSMETL WQSRCEQLPP GALQLLRRIA AAGRQLPVEE LRVWDEDASS LEDHLDELQR RRLIVRGESS GPTVQIWHSR LGERILDQMS EPDIRQLHLD WAETLSHVRP DVANVIASHY QRAEAHEPLA EWAKLAAEQA QQMFAHREVA SWLQVAADHS DGEQRIAYLK EASFAWHRSG LLSNAAMTHE ALAKLLDGHA SVEQELHRVE CLIRSGEFSD ASRLVEPLID QLGLPRLKSK WAFKLSVIWR IIRLLPMQRD LTGLLDQPSP LRTWQEGSQI EACNRLIRPL SIINNNIAVE WSLFAARQVR LLGTAGERLQ LGVGEAVFNC YSPGKSRQRA GQILERMSGA LKPEDDPSWH ADVNSGLAWH AAMDGRYADA LAPCARSKKF YALSEHAKNF EIAHTSYVEL ASFFQCGMIS EIRKSVAEMQ AEGRTTNDQF VTIMGTLGYA SVAFFSDNDL ARMDLASDRV RECMKQVGAT SFLFVQQFKD VLHDLYAADV TNGASKLDLL PRQMQLTDLN RVQMIRINFL EFVCLLALQA LSCKTKTAET VLQRSLRKLR RERSEFAKMK ADFYEGIQMA RSPVAGMDVH ARERLVAAHA KAEELRLTPF VLAASDELKW LEDISQPSDL EAYLADEGVV APSRFARLYR GVERPEG //