ID J1S797_9ACTN Unreviewed; 798 AA.
AC J1S797;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=PQQ-binding-like beta-propeller repeat protein {ECO:0000313|EMBL:QTZ93373.1};
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EJJ06707.1};
GN ORFNames=SU9_019445 {ECO:0000313|EMBL:QTZ93373.1}, SU9_12147
GN {ECO:0000313|EMBL:EJJ06707.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ06707.1};
RN [1] {ECO:0000313|EMBL:EJJ06707.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ06707.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ93373.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ93373.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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; AJGV01000081; EJJ06707.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ93373.1; -; Genomic_DNA.
DR RefSeq; WP_006603991.1; NZ_CP072931.1.
DR AlphaFoldDB; J1S797; -.
DR STRING; 1160718.SU9_12147; -.
DR KEGG; sauh:SU9_019445; -.
DR PATRIC; fig|1160718.3.peg.2460; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_000288_135_1_11; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000009036; 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; 2.40.10.480; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-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:EJJ06707.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009036};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EJJ06707.1};
KW Transferase {ECO:0000313|EMBL:EJJ06707.1}.
FT DOMAIN 22..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 276..390
FT /note="Disordered"
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 798 AA; 83208 MW; A16896547E1D077D CRC64;
MPALRDSGLG PEAEHPEYAG QYRLEARLGA GGMGVVHLAR SSSGLTLAVK VVHAEFAQDP
EFRGRFRQEV AAARRVSGAF TAPVVDADPD AELPWMATLH IPGPSLSDHV KRNGPMVPGE
VRQLAAGLAE ALRDIHRAGV VHRDLKPGNV LLAADGPKVI DFGISRPSDS EMRTETGKLI
GTPPFMAPEQ FQRPREVGPA ADVFALGSVL VHAATGRGPF DSESPYLVAY QVVHDEADLA
GVPEELAPLI EGCLAKDPAD RPTPDALMEL LRTASFGETP PGRAPLGQTP PGEPPSGEAS
GSAPPHAPIP GQRQPVRTGA TPPRAETTHV RAPVPPEITT GPGHSPDSGP GPGPGSDSGP
AHPAAPSRST DSRRPTGPRR PTRNTRPRTR RWPLWAALAL VVTGAGTFAG IRALAPAGDG
QDPALQIHPS RAEAANFRPW HTTLTKRPKG YAAELPFCTT GSGAVFCGRA GVLAARIDPG
TGQVAWRRKD AAATGKNSLK TMASPTPPAL SGGLLYVFSA DAKRLLALDP SADGKGATRW
SKDVSGYEGG ARIVGDQVLL TAADGTVTAL DSATHRQLWH KRFPGHTLPA FTAFGAPHTA
YAAENSPDGT STQVTAIDPA HGSVRWSHRL PGLLSVAGPG TSGALYLTVT DRTFSYRATA
VLRYDPATGH TRRLKLTAPL DGASAVVHGD SVFLLAEGGA LQAVGERTWD TETSVSRGSA
PVVSGGRLYF TAADGRLLAV DTRSGALLGQ TPPRMNGRHN GFVEMLPAPL VDGRRGRVYA
AAPDGSVFSA PAGDPAGW
//
