ID L7FJ52_9ACTN Unreviewed; 616 AA.
AC L7FJ52;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Kinase domain protein {ECO:0000313|EMBL:ELP70730.1};
GN ORFNames=STRTUCAR8_01135 {ECO:0000313|EMBL:ELP70730.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP70730.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP70730.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP70730.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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 -!- 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:ELP70730.1}.
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DR EMBL; AEJB01000041; ELP70730.1; -; Genomic_DNA.
DR RefSeq; WP_006373904.1; NZ_AEJB01000041.1.
DR AlphaFoldDB; L7FJ52; -.
DR STRING; 85558.T45_03075; -.
DR PATRIC; fig|698760.3.peg.633; -.
DR Proteomes; UP000010931; 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-EC.
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 InterPro; IPR026004; Septum_form.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13845; Septum_form; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ELP70730.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Transferase {ECO:0000313|EMBL:ELP70730.1}.
FT DOMAIN 21..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 287..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 616 AA; 64737 MW; AE9B405FAB49D59E CRC64;
MPSGPSGPPA SGVGRVIAGR YLLLNQLGSG GMGHVWLAHD QELACEVALK EIVFRDPVEA
SDERASRVAR ARAEARHAAG LRANPNVVTV HDVLEHEGLP WIVMEYVAGA LDLRDLIGMR
GPLAPDECAR IGLAVLDALT AGHEQGIMHR DVKPANILLA PDRTGTPYSR ILLTDYGISV
QPDAGETRYT LTSALVGTAG YLAPERATGG PPTAAADLFS LGCTLYHAVE GVGPFERDTH
FAEVTAVVME EHRKPERAGA LRPVLEAMLD KDPDRRITAA RAEAALDRIV TPQADPYEHT
RTDPGSLPPW GASEQLYGPH QAPPSPPVGV SPARSAPPPE PPRHTRALPA ALGALLGIAL
AGAGLWFVLG GPPGGDEETA RKPYGGPVGL AAPLAVGDCV FADWPGGARF EGTPRLTVDP
ACGGAAPDGQ VLAVVDAASA AEARVRGPGE CEERTRDLRE KLADVRGYAV VPAEGGFRAA
EGRTACLLLG ANGPVYGPLG PFREAGQAFR DTAGMQKRDC LRSPSGREAR LVACTEPHDE
QVLGFTRLDA AVPFEEARDV SDTACAKAVP PTDYGFDPSV YEAGSWTGRG AWDSGTHFVV
CTVRRQNGGT MEGEEP
//
