ID H6RML4_BLASD Unreviewed; 331 AA.
AC H6RML4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=BLASA_2978 {ECO:0000313|EMBL:CCG03849.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03849.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG03849.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG03849.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) 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; FO117623; CCG03849.1; -; Genomic_DNA.
DR AlphaFoldDB; H6RML4; -.
DR STRING; 1146883.BLASA_2978; -.
DR KEGG; bsd:BLASA_2978; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_072253_0_0_11; -.
DR OrthoDB; 4088450at2; -.
DR Proteomes; UP000007517; Chromosome.
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 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:0000313|EMBL:CCG03849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:CCG03849.1}.
FT DOMAIN 21..164
FT /note="MEDS"
FT /evidence="ECO:0000259|Pfam:PF14417"
FT DOMAIN 206..324
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 331 AA; 35620 MW; FD1C7B293B490F07 CRC64;
MQVDWTTTGG AGRPAPGGFP HDALLYDSTE QLVALAAPFL RAGLAEGDAA VVATRPDTAA
ALREALDDDP RLQVVERHAV YRPRTPEAIT TFRRLAEQCT AAGAGRVRVV GEADYGRTER
DWLEWERYES VINRALSGWN LWGLCAFDTR QLPDPVLESA GRTHSRLVTA DGRVPSPSYT
DPAAYLRTLP IPDEPLERTP PRLAAADVRD FIGLRHAVAA ELAGVPAGAD LVDDFLLAVD
EMASNAVRHG LPPVSLRLWT GADRIVCTIT DGGPGWDDPF AGYGPAHGSD LSRGGMGLWL
ARQLCDHVDI AGGDHHPGGE TVSVRLTTFL R
//
