ID A0A0N1NA23_9ACTN Unreviewed; 172 AA.
AC A0A0N1NA23;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=OK006_1631 {ECO:0000313|EMBL:KPH96929.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPH96929.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPH96929.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPH96929.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) 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}.
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:KPH96929.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJCU01000291; KPH96929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NA23; -.
DR PATRIC; fig|1592326.3.peg.11386; -.
DR Proteomes; UP000037912; 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:KPH96929.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:KPH96929.1}; Transferase {ECO:0000313|EMBL:KPH96929.1}.
FT DOMAIN 32..145
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 172 AA; 18623 MW; D8F724A9880DCF88 CRC64;
MGTNGSTMLE PLRQGLPPLD PAAVSSAASC ALPARYEAVR EARQFTRRTL DQWDIGERFD
DVCLVVSELV TNALRHALPS DTPRSDDQGP PVRLHLMRWT SRLVCAVRDP SHDSPVAGDS
EDFSAESGRG LFLVDSFADS WGWHPLAGTL SGKVVWALFR LPQPAAGGVS AE
//