ID C9ZEX0_STRSW Unreviewed; 791 AA.
AC C9ZEX0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:CBG68903.1};
GN OrderedLocusNames=SCAB_17731 {ECO:0000313|EMBL:CBG68903.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68903.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG68903.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG68903.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG68903.1; -; Genomic_DNA.
DR RefSeq; WP_012999627.1; NC_013929.1.
DR AlphaFoldDB; C9ZEX0; -.
DR STRING; 680198.SCAB_17731; -.
DR GeneID; 24313441; -.
DR KEGG; scb:SCAB_17731; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_1_11; -.
DR Proteomes; UP000001444; 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; 1.
DR SMART; SM00564; PQQ; 4.
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:CBG68903.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CBG68903.1};
KW Transferase {ECO:0000313|EMBL:CBG68903.1}.
FT DOMAIN 15..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 330..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 791 AA; 82678 MW; B5542D496ED283E9 CRC64;
MEPLGSDDPE ELGPYRLVAR LGAGGMGRVY LARSPEGRTV AVKAIRPELM GDKNFRVRFR
REVEAAGAVG GRYTAPVVDA DPDGPVPWLA TDYIAGPTLA EAVAAHGPLP VESVLVLGAG
IAEALISVQA AGLVHRDLKP SNVLLAADGP RVIDFGIVRA SDGYDLTRSG ALFGSFEYMC
PEQATGEPLG PEGDVFSLGS VLTFAAAGHA PFSGTAAATL LYQVVHTAPD LTGVPEPLDR
IINLCLTKDP RLRITPDKLA AACAPGGVEQ LAENGWLPAS VASSIALRAA AVRTLDTTPY
AEVVFPSAGS GPEPDVYAAR RSGAAYDFER DEEAGAAGSP SAPDPARPYD GSGLPGGSAR
ETSPGGSGEA RSGAEDRTGA APLSPPGGPE PYRAPGHRRA VSRPGMSRRT VLSLSAGSAA
AAAVGAALVL GRPDEPAARS TKPAGPAPKP LWTYRGGPML QAPAVFHEGT ALVKTRPGDL
VCLDLKDGTR PKWVYEGISQ SPTPTVLAFD SAIALGEGAT VIGVDPADGT ERFTIDFGPD
NRFDTLLGAT ADRWVSVTGV RLRRESARQG VATSTDTVFG VDLAGRRAEV IPISPEDVGV
RLAPVILPGF FVYADGLRNV TVRSTDSSGV LWRHPVGYDL RPGLAVLDRT VFAISRHLEA
LNLATGKVRW RVKPERGMFA SLGGYGNTIY VTGTDPAGVY AFNAGTGARR WFCPTPRLNI
DQPVTAGPDA VYVPAYQNRD GIYAIGAAKG RLLWNFTDGV ETGVNDWQLA CDHSGVLVAQ
HYDRTYGLPA P
//
