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Database: UniProt
Entry: A0A3Q8VBP7_9ACTN
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ID   A0A3Q8VBP7_9ACTN        Unreviewed;       174 AA.
AC   A0A3Q8VBP7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, 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=DLM49_16620 {ECO:0000313|EMBL:AZM60963.1};
OS   Streptomyces sp. WAC 01438.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM60963.1, ECO:0000313|Proteomes:UP000271045};
RN   [1] {ECO:0000313|EMBL:AZM60963.1, ECO:0000313|Proteomes:UP000271045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM60963.1,
RC   ECO:0000313|Proteomes:UP000271045};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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; CP029601; AZM60963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8VBP7; -.
DR   OrthoDB; 3479886at2; -.
DR   Proteomes; UP000271045; Chromosome.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; 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.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271045};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          51..156
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   174 AA;  17702 MW;  7CC5E91AF1C94432 CRC64;
     MRQHTSTSPR RPGGVLDRDA GRPTSDPGQG LVTGDGTTTL ITDLPYGPEA AEVARGAVTL
     ALRGAETDVL ADARLIGSEL ATNAFVSGSP PLVLCVDRRS LASGGLEIEV TVTDGGCPRP
     APASPTAPDE QAESGRGLVI VDALADAWSL TTGTNGSRAW CRLAHRPCSS SAGT
//
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