ID A0A0F7NF74_9ACTN Unreviewed; 562 AA.
AC A0A0F7NF74;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AA958_32260 {ECO:0000313|EMBL:AKH86124.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH86124.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH86124.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH86124.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP011492; AKH86124.1; -; Genomic_DNA.
DR RefSeq; WP_047019352.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7NF74; -.
DR STRING; 444103.AA958_32260; -.
DR KEGG; strc:AA958_32260; -.
DR PATRIC; fig|444103.5.peg.6811; -.
DR OrthoDB; 4652229at2; -.
DR Proteomes; UP000034283; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR005467; His_kinase_dom.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 266..375
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 381..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 58678 MW; B7F6CE1A464DBA33 CRC64;
MDPAGPATGG RRTGFVRWWL IPTAVVVVST AIALPLVSAD ARTPVAVCGA IATLVVAFAA
AEAERRGRAA GAPSAEQADH EAAWERRLAA REAEMIRLAG LLPQAVARLQ RGEYAEDVLA
DIEAEKSLTP QVRAAHAAAL RSVVEAVQDA EDLRVSAERG FVNIARRVQA IIHQQARSLR
EMEDRHGRRH EFFADLLKLD HGTALVGRLA DSIAVLGGDR PGRQWGKAIA LYSVLRGGMS
RIIDYQRVEL HPVAEVAVVG SAVEPLIHAV AELLDNATRY SPPHAKVHLS ATEVQSGVAI
EIEDGGVGLS EEARERAEHM LAEAQAGIDL NDLGETPRLG LAVVGRLAQT YDFRVSLRPS
AYGGVRAVLV VPQVLLTTTP ATGTAHGIGA TSGPRPLRNP TPPPAGVEGS ADARAGLKRS
RDRVPPARQA GPQPSPPAHP EPVAGSLPQR RRRAPVAPPA APAAGGQPSG RRTATASPAG
TENGAAEVRG VEPGLWLGDF TRGLEGEPQG GDAGAAAEPQ EPGGTARGED EAAGSIRPER
PARLRHGDGA PGPSNPSSGE ED
//
