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Database: UniProt
Entry: A0A1M5Z382_9ACTN
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ID   A0A1M5Z382_9ACTN        Unreviewed;       179 AA.
AC   A0A1M5Z382;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN05444521_5036 {ECO:0000313|EMBL:SHI18712.1};
OS   Streptomyces sp. 3214.6.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHI18712.1, ECO:0000313|Proteomes:UP000190947};
RN   [1] {ECO:0000313|Proteomes:UP000190947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; LT670819; SHI18712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5Z382; -.
DR   STRING; 1882757.SAMN05444521_5036; -.
DR   Proteomes; UP000190947; Chromosome i.
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.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:SHI18712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190947};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:SHI18712.1}.
FT   DOMAIN          9..132
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   179 AA;  18540 MW;  0395882326B1EE27 CRC64;
     MLKVQLEIRP DPAEVGRARR WARSRLAGSG IGDEEPLAET LILLVSELVT NAVVHTGCPA
     VLRLSLPSVS EGEAADDPAE PSIVRLEVAD ISDRAPVPRC AGDDATGGRG LALVDGLADR
     WGWSVEGAGK RIWCELDRCA GSDAAAVGHG SAVGHENATE CASAAGQESA CEGFAFEVV
//
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