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Database: UniProt
Entry: A0A250VL80_STROL
LinkDB: A0A250VL80_STROL
Original site: A0A250VL80_STROL 
ID   A0A250VL80_STROL        Unreviewed;       320 AA.
AC   A0A250VL80;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=SO3561_06527 {ECO:0000313|EMBL:GAX54973.1};
OS   Streptomyces olivochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1963 {ECO:0000313|EMBL:GAX54973.1, ECO:0000313|Proteomes:UP000217446};
RN   [1] {ECO:0000313|Proteomes:UP000217446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3561 {ECO:0000313|Proteomes:UP000217446};
RA   Dohra H., Kodani S.;
RT   "Streptomyces olivochromogenes NBRC 3561 whole genome shotgun sequence.";
RL   Submitted (MAY-2017) 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:GAX54973.1}.
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DR   EMBL; BDQI01000016; GAX54973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250VL80; -.
DR   STRING; 1963.AQJ27_28550; -.
DR   Proteomes; UP000217446; Unassembled WGS sequence.
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   InterPro; IPR025847; MEDS_domain.
DR   InterPro; IPR047718; RsbA-like_anti_sig.
DR   NCBIfam; NF041045; RsbA_anti_sig; 1.
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   Pfam; PF14417; MEDS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217446};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          22..165
FT                   /note="MEDS"
FT                   /evidence="ECO:0000259|Pfam:PF14417"
FT   DOMAIN          206..314
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   320 AA;  34877 MW;  8AADC98082AD7A0A CRC64;
     MEQGEDGARS PLVRDRAEPF AHPALLYRSE QEYAQGTLPF VSEGLATGLP VAVAAPPSRL
     ELLKAELGPA AHEVRWIDMT RAGRNPGRII PAVLRSFADA HPGRPVRIIG EPIWYSRTPL
     EYPACVQHEA LINAAFHGRE ATILCPYDAR TLSDDVIADA HATHPVVISD GRQAVSHAYD
     PERVLARYNE TLPYPPGAAT VRFTAGLLPA VRDIALREAR ERGMAPPRLQ DLNLVVAELT
     TNSVVHGGGS GTLRIWAESE QIVCEVRDEG HLTDPLAGRR PVRPDQLGGR GLLLVHFLSD
     LVRVHTAASG TTVRSYLARR
//
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