ID A0A1I5N6G0_9ACTN Unreviewed; 149 AA.
AC A0A1I5N6G0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=SAMN04489713_11228 {ECO:0000313|EMBL:SFP17172.1};
OS Actinomadura madurae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1993 {ECO:0000313|EMBL:SFP17172.1, ECO:0000313|Proteomes:UP000183413};
RN [1] {ECO:0000313|EMBL:SFP17172.1, ECO:0000313|Proteomes:UP000183413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43067 {ECO:0000313|EMBL:SFP17172.1,
RC ECO:0000313|Proteomes:UP000183413};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 anti-sigma-factor family.
CC {ECO:0000256|ARBA:ARBA00037972}.
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DR EMBL; FOVH01000012; SFP17172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5N6G0; -.
DR STRING; 1993.SAMN04489713_11228; -.
DR eggNOG; COG0642; Bacteria.
DR InParanoid; A0A1I5N6G0; -.
DR Proteomes; UP000183413; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR PANTHER; PTHR35526:SF3; STAS DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SFP17172.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183413};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:SFP17172.1}.
FT DOMAIN 40..145
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 149 AA; 15939 MW; 388C37D405D9B050 CRC64;
MGINALNSGE LDMSCVAARS TAGLVRTLVE FRLCEWGLTR IAGDVRQVAG ELVANAAEST
PGREIRVRFT REPRAVTIAV WDASDAMPVA QPIVELVLDD LVPDARALEP GHDAGMRGRG
LPIVQALSAD CGVTRTDPCG KWVWAKVAF
//
