ID   Q7UW31_RHOBA            Unreviewed;       797 AA.
AC   Q7UW31;
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=RB2299 {ECO:0000313|EMBL:CAD72540.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD72540.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD72540.1, 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};
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DR   EMBL; BX294136; CAD72540.1; -; Genomic_DNA.
DR   RefSeq; NP_864856.1; NC_005027.1.
DR   AlphaFoldDB; Q7UW31; -.
DR   STRING; 243090.RB2299; -.
DR   EnsemblBacteria; CAD72540; CAD72540; RB2299.
DR   KEGG; rba:RB2299; -.
DR   PATRIC; fig|243090.15.peg.1054; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_352627_0_0_0; -.
DR   InParanoid; Q7UW31; -.
DR   OrthoDB; 279610at2; -.
DR   Proteomes; UP000001025; Chromosome.
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; cd00130; PAS; 2.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50112; PAS; 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:CAD72540.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Transferase {ECO:0000313|EMBL:CAD72540.1}.
FT   DOMAIN          147..419
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          534..580
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          63..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   797 AA;  87729 MW;  D8D56C5703DA6FBF CRC64;
     MMPPSDVLMS SLIETIEVDA ALANRLAEMP ADSQTLTLSL DAIANGGSTA GVLQHPSWAR
     NPHLLTPLQS TGADDSEDEL SETIEVSGSV GPVEGSSPAG GNLLSNDPID GQSALASCEG
     FLPPRRIAML SSDPTKADCV SLKDVEYRLI GTLGSGGTGI VYQAHQRAID REVAIKVLRR
     ELATDASSRG RFLAEARVIG ALDHPNVIAL HDLCIDDEGQ LFYSMKRVDG ASWDQQIDTL
     SLEKNLNILL RVADAIRYAH SRGLVHRDLK PENVMLGRFG EVLVADWGLA LSKSSLTPSS
     AVPSTDSHHA IGGTPAYMAP ELAAGDLFGI TYATDIYLLG AILFRVVTGF PPHHGKSLLA
     CIRAAANNKI EPIPENLGDT ELELIQIAHK AMATEPLDRF TSVEELIEAI EGHRSHEASD
     RLVRRAKRRL AELDELDAVE DPNKEKGSSG LRADRYERFA AVDALLREAI EIWPDNRRAI
     DTLRSTQLEF ARTATAQGDL DLALVLYESA GQSNSEAAAR VRKQRDRRER VRESQAKYST
     LFTHSPDAGL LIRWSDGVVM EANTACLELL GYEKEEVVGE KMTSLTIWAC PMAREKFIDQ
     LAREGQIDNF ETQFVPKQTK LENPICDDHP VDRSEVKGLI DVLISSRTVQ LAGEEMLLST
     VRDISARKAA EHDLEYSRRR LRDLQRLAGL GSWSFTLQSQ AIHWSEEAFR VTGRDVRRGS
     PNYNEFVASI HPDDRESLQI AIERSVTQGT SYQLKFRYRD DQGKYRKLFT RGNPVFDADD
     NVIEIYGILQ HVAAGGG
//