ID   Q7UZ75_RHOBA            Unreviewed;       987 AA.
AC   Q7UZ75;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=RB140 {ECO:0000313|EMBL:CAD71408.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD71408.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD71408.1, 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; BX294133; CAD71408.1; -; Genomic_DNA.
DR   RefSeq; NP_863737.1; NC_005027.1.
DR   RefSeq; WP_011117760.1; NC_005027.1.
DR   AlphaFoldDB; Q7UZ75; -.
DR   STRING; 243090.RB140; -.
DR   EnsemblBacteria; CAD71408; CAD71408; RB140.
DR   KEGG; rba:RB140; -.
DR   PATRIC; fig|243090.15.peg.78; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_302241_0_0_0; -.
DR   InParanoid; Q7UZ75; -.
DR   OrthoDB; 9801841at2; -.
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; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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   InterPro; IPR011990; TPR-like_helical_dom_sf.
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   SUPFAM; SSF48452; TPR-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:CAD71408.1};
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:CAD71408.1};
KW   Transferase {ECO:0000313|EMBL:CAD71408.1}.
FT   DOMAIN          148..463
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          331..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   987 AA;  106568 MW;  9B2E604C194361E6 CRC64;
     MNLSDLPARE LARLDAVCLE YESSLRQVAD GEPAPSDLTS IQSLVERHGG EHADLLRSEL
     EAIRAEIDGD LGIHGDSGEL TQVLAASNDT PSREAAALDT PAVDAMKMDD SLRSTPSAEA
     RVKKALAKVA SDGSSDSLPP LGTEIGPYRL DGVLGRGGMG VVYRATDTRL ERSVAVKMLS
     IDGHPNLVER FQREAKAVAS LTHPNIVELF DVGVHEGMPY AVMEHLRGET LMRRMESRRT
     DVAPITTQMV RYWGRQLAEA LATSHASGVI HRDLKPENVM LVGRRSGSPT PSPANSNTIS
     GHSIAMQSSN ETSLPSVKLF DFGLSRVGRA VFGPGESDPE SQHEDAGNDE ANEAKTRAGM
     ILGTPGYMAP EQARGETVTP AADVFSLGCV LFEAFYGRPA FTGKSPASRY AAVLEKTPLP
     DPGRRRDDIA LADLIMAMMR KVPAERPTAA TVVAALSSGG AILPANDGET LATPMDGASM
     TQPIRIAGGV SRRRFVEMIG GSFAGALVGM SGLSGNWAKL NRIRSIGVLS FTPATQVETK
     NEVDPQPARG RMLQRGELLA GLVANELSRL EGLSVPKYVP MTASFPDQYR DAASRLEVDA
     LVTGTFTEAT GAQPGFMDVN IQIICAESGT QIWGKVIRTS GGDNLIEQNH LARQVASAIN
     RSLLENPHES RPRDPGAFTC LLKGRTQADP DSIDGMRSAL KCFDSALSED PNYAPAHAGK
     GLTSLTLAGR VADEEAQELI IQAQRSIESA LELDTTNVEA RLASAMLMYQ RLGDLKPARD
     ILLALSKEAN NSWQVFHQLG WVQLMLYEEM AGVVSLRRAA SLHSTSKLLQ SDLARAQWFV
     ANKRRAIDEA TGVMPKTDGN QVGPESFTRG LLIDLYEHSS DLKLAADLDP GLNWSESDGA
     DRYWELREAR LETLPYGPYG PTLNETILQL RRTDVVTREP AEQRLARLLQ TRSPMLPLLL
     IKHPQFDSIR TLPAAGEAFP VLRPGVV
//