ID A0A1Q5E771_9ACTN Unreviewed; 714 AA.
AC A0A1Q5E771;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:OKJ03963.1};
GN ORFNames=AMK18_01925 {ECO:0000313|EMBL:OKJ03963.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ03963.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKJ03963.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKJ03963.1,
RC ECO:0000313|Proteomes:UP000186839};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 leucine-binding protein family.
CC {ECO:0000256|ARBA:ARBA00010062}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKJ03963.1}.
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DR EMBL; LISW01000001; OKJ03963.1; -; Genomic_DNA.
DR RefSeq; WP_073861392.1; NZ_LISW01000001.1.
DR AlphaFoldDB; A0A1Q5E771; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000186839; Unassembled WGS sequence.
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; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028081; Leu-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF13458; Peripla_BP_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:OKJ03963.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000186839};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OKJ03963.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:OKJ03963.1}.
FT DOMAIN 15..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 714 AA; 74149 MW; F3EC5B6331978AEA CRC64;
MEKLRPSDPA RIGGHRLLGR LGAGGMGVVY LGRTDAGTLA AIKVILPEYA ADDDFRTRFR
REAEAARRVD SPWAVPVSGA DTEGERPWLA TAFVPGPALS EAVARCGPLP PRAVRVLGRL
LARALAAVHA AGLVHRDVKP GNVLLTVDGP RLIDFGIARS VDATALTGTG LVVGTPGFLS
PEQATGGGTE AGPASDVFSL GCLLAYAATG RPPFGSGAVD ALLYRTVHDE PDLAGIEDPE
LRALLDTMLA KEPGTRPTAA ALDTRITEDA PDGSIDWLPA DVAALVAERS AAVLGLPGAD
PTIADSAARS GPGRRRALLI AGAGLVVAAG GGFAVREWLR DDSGSDAAAP GERAWIIGVQ
ADLSGPRSAA GRAQERGVRL AVQQFNARAD KPFTLTVAVR DDGGDPARGV RAATGFARDR
DVLAVVGPTG DAVTEAVLGT YDEAMLPVLT VSSLQLTYAA RARKSFFQAA PADGVLAQPI
IRRLVLRPEV ERLGVLLDRS GGHSAYQVGY LTNMMTGELT TGTTYPRVVP AGTRDLAPVV
EDMLAHASDA LFYAGDAAGA ARTARALAAT SFKGPRMAMH TAMDARFLKD AGQAAEHWEF
TAPFTDPAAP AAKKFAAAHR AAFDTAPAHW AAEAYDAAGM AIAAVTALAG TTAGRPKRPS
RSALVTKIAA STYEGVSRTY AFDENHRIKG DDAHLYGVRD GRYVYLGAAP KATA
//
