ID   Q7UF57_RHOBA            Unreviewed;       417 AA.
AC   Q7UF57;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   SubName: Full=Probable serine/threonine protein kinase {ECO:0000313|EMBL:CAD78826.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:CAD78826.1};
GN   OrderedLocusNames=RB10329 {ECO:0000313|EMBL:CAD78826.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78826.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD78826.1, 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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; BX294151; CAD78826.1; -; Genomic_DNA.
DR   RefSeq; NP_869369.1; NC_005027.1.
DR   RefSeq; WP_007334318.1; NC_005027.1.
DR   AlphaFoldDB; Q7UF57; -.
DR   STRING; 243090.RB10329; -.
DR   EnsemblBacteria; CAD78826; CAD78826; RB10329.
DR   KEGG; rba:RB10329; -.
DR   PATRIC; fig|243090.15.peg.4995; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_658681_0_0_0; -.
DR   InParanoid; Q7UF57; -.
DR   OrthoDB; 6111975at2; -.
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:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd17574; REC_OmpR; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52172; CheY-like; 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.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAD78826.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CAD78826.1};
KW   Transferase {ECO:0000313|EMBL:CAD78826.1}.
FT   DOMAIN          2..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          138..406
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   417 AA;  46756 MW;  402C9992BEEB04BA CRC64;
     MKLLIADDNP VWRNLISAAV ENWGYRIELA SDGNEAYELL QSDDPPRLAL LDWLMPGMEG
     VEICRRIKQD PENPFTYIIL LTSRDRDEDM IQGLDAGADD YLTKPIVAPL LKSRLTAARR
     IVEAVPPMKW TKPQIEGFDI DHLIGRGAFA TVWKGMHRAS GKPAAIKIIR ADLATDLVFE
     RFAREIQVMR KMDHPGIATI YASHLERDLA YYAMELIDGE SLANYIARES PRATRIIEMM
     AMVCDALQHA HDHGVIHRDV KPSNIMVGPD EQPKLVDFGL SKSMFRTKSP VSANSTHDGA
     VLGTPLYMSP EQARGDANSV DHRSDLYAVA TMLYLFLLRE HPHGALSLSR EETIDAIANT
     DPRPATEINP KFNPKLESIL SRCLSDDPEE RPQSAGQLAQ ELRDFLNDRA ALRTQTL
//