ID   Q7UFU9_RHOBA            Unreviewed;       780 AA.
AC   Q7UFU9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Probable serine/threonine-protein kinase pknB {ECO:0000313|EMBL:CAD78581.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:CAD78581.1};
GN   Name=pknB {ECO:0000313|EMBL:CAD78581.1};
GN   OrderedLocusNames=RB8326 {ECO:0000313|EMBL:CAD78581.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78581.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD78581.1, 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   -!- 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; BX294147; CAD78581.1; -; Genomic_DNA.
DR   RefSeq; NP_868303.1; NC_005027.1.
DR   AlphaFoldDB; Q7UFU9; -.
DR   STRING; 243090.RB8326; -.
DR   EnsemblBacteria; CAD78581; CAD78581; RB8326.
DR   KEGG; rba:RB8326; -.
DR   PATRIC; fig|243090.15.peg.4012; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_358975_0_0_0; -.
DR   InParanoid; Q7UFU9; -.
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: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; 1.10.510.10; 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   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:CAD78581.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Transferase {ECO:0000313|EMBL:CAD78581.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        384..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          72..336
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          43..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   780 AA;  83854 MW;  EF24FD9B038A7418 CRC64;
     MCQCLPCRVG FCRTSWAGRL ASRSTASTTG GMHWFPIATR HLMTDSPPAP DSPPEFLDPP
     EAAGELGRLG PYRVIELLGQ GGMGHVYRAQ DTRLQRTVAL KVMNERFAKS PNSRKRIVEE
     ARSMAAVHHD NVATLFEVGQ RNGTPFLAME LLQGGTLEQL LQSGRQFSSE EVIAIADQVA
     LGLEAAHDRG IIHRDIKPAN LWIQSPSERV KILDFGLAVA GSAVQGLARG DSVVGTPGYL
     SPEQARNETV DERTDLYSLG VVMYEMCAGK VPLLASNTPT QLVNILCREP LTLSQRKQNG
     ESVEVPEPLE RLIMRLLSKE PGQRYETAGH FRKALLAVSE QIQQSKQAGL AIDIDANSSN
     GSSVPAGAEP AATTKTTSGG TGKAFFAAVG LAVAALIAGG VWWMLRDGTS KSTSMESVKS
     ASTPDTSPAV LAAELGALQL TGKVIADPEI PVGEMARFRL QLTNQADSRE SDPRIRYSQA
     GQVARITTYL QQEGQLKRKA PAFPRSFSPR QLPGPGETQS IEIQFLTNNL AQERFDVIFE
     LQSPAGAHVD SLTSQFEVTE NLQTGDLLGF ETIRTRAGKG ADTYVREGSK EDFGKQPAVM
     AHRDGANDQN VLAIAFLRFD LTQLPPPSGA GADSASAVLK RIDRSALLLS MAPNSHPGVG
     RILVHGWPSD LTTPGGIGSL DWSETGEASL TFETSPVANG VGDLVPLGEL KFDNSGEGLK
     DQPDGLRFVS RALDDFLRSS PGVVTLVLSQ EGWLGDPTRF NSRDRSPELA PGLAVRWKTD
//