ID K4R5K2_STRDJ Unreviewed; 698 AA.
AC K4R5K2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:CCK28382.1};
GN ORFNames=BN159_4003 {ECO:0000313|EMBL:CCK28382.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK28382.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK28382.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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}.
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; HE971709; CCK28382.1; -; Genomic_DNA.
DR RefSeq; WP_015658734.1; NC_020504.1.
DR AlphaFoldDB; K4R5K2; -.
DR STRING; 1214101.BN159_4003; -.
DR KEGG; sdv:BN159_4003; -.
DR PATRIC; fig|1214101.3.peg.4053; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_000288_135_1_11; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CCK28382.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CCK28382.1};
KW Transferase {ECO:0000313|EMBL:CCK28382.1}.
FT DOMAIN 22..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 698 AA; 74075 MW; 49CEDB0079BB3E4F CRC64;
MAPQRNAGAG AEAELPEYAG HYRLESCLGS GGMGVVHLAR STSGMKLAVK VVHAEFARDR
EFRGRFRQEI AAARKVSGAF TASVVDADPD AERPWMATLF IPGPTLSDQV KRNGAMAPEQ
LRRLMAGLAE ALRDIHRVGV VHRDLKPSNV LLAEDGPKVI DFGISRPKDS ELRTETGKLI
GTPPFMAPEQ FRRPREVGPA ADIFALGSVM VHAATGRGPF DSDSPYVVAY QVVHDEPDLT
GVPENLAPLI GRCLAKEPED RPTPDELMRE LRSVAASYDT QAFIPAQRTS PEPKAPRVPA
EKPEVRRRLG KFRGRRTALT AAVLALVMGG AFTAVRMAGD EPAPAGNGTG KTSAAFSSWE
TASVSGSATV PQCSYGASKL LCAQSGVVFA LDPLDGRVLW RHAVSGTRVG PPAVTGGLVH
PWLDLSRSLK ALDPATGKPK WQRDVPPYSG LAYAGGSLLL TGTDGAVSGV DGATGAPRWS
HHVPGHELPY FASFPGDPLA YAISRSQDDA TTRVTAVEPD TGDVRWDALL DGALKPVGTA
DGSVYFVALG KVYEDATSVV RYSPDTKNSV RVELPVPVQQ PEGTVRGDVV YLLGNGGSLV
AVDMDARRQR WSTETGVTRG SAPVTDERHV FFTALDGRLL AMDAQDGSLA GQTPPRLGSK
PDQVAVGLPA PVIVGRHIYA SAPNGSVFAV DARNPSTW
//
