ID A0A117KBH7_9ACTN Unreviewed; 541 AA.
AC A0A117KBH7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-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=ADL25_05185 {ECO:0000313|EMBL:KUJ55815.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ55815.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-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:KUJ55815.1}.
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DR EMBL; LMWH01000026; KUJ55815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117KBH7; -.
DR Proteomes; UP000054048; Unassembled WGS sequence.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR PANTHER; PTHR35526:SF3; STAS DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 31..189
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 541 AA; 56728 MW; A835506203617CA2 CRC64;
MMTYSPHASA RRHVSPARDA FDIARQLVDS AVPDLADIAA VEVSDALFDE RSALSEAGAC
QGFRRAAFRA VCGHGSRCAY RIGEVSRIPS GTPYRRTLSD RRPRVIASLP PQAHWLARDP
ARAPLMHQDG VHSLMVVPLV AHRVVLGLVA LYRCNGSSPF GKAELRAAAR LAGRVARMLD
DVHRDLREQA MGRILQHALL ARPPHLTAVE DVRGHVPADG APGGWFDVIP LPGTRVGLSV
GSTGGRGIAA AAVMSQQKAR VAALAALDVE PVEALTHSLR PSTVTATPPP VEGPAADRSS
AQTHCLYAVY DPVTRRCTAA RAGAAGLTVV APDGDVTSVG PTASDAADGD GYDVAVFDVP
PGSLLVLSCA GAPEQRGDAS DDQEARNGAC TGGDARLPLT GRGAHVLLTA RTRAVAPMDI
ATWELPNDPT AVADARDRTA TQLTAWGLPD LSFNTTLVVS ELVTNAIRYS TGPIGLRLIR
DAALICEVSD NSSAAPRTHI PAPNDQGGRG LIIVAHLARA HGTRYTAPGK IVWAEQAIDV
A
//
