ID A0A5J6HK46_STRAD Unreviewed; 555 AA.
AC A0A5J6HK46;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CP975_26900 {ECO:0000313|EMBL:QEV20689.1};
OS Streptomyces alboniger.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=132473 {ECO:0000313|EMBL:QEV20689.1, ECO:0000313|Proteomes:UP000326553};
RN [1] {ECO:0000313|EMBL:QEV20689.1, ECO:0000313|Proteomes:UP000326553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12461 {ECO:0000313|EMBL:QEV20689.1,
RC ECO:0000313|Proteomes:UP000326553};
RA Lee N., Cho B.-K.;
RL Submitted (SEP-2017) 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};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; CP023695; QEV20689.1; -; Genomic_DNA.
DR RefSeq; WP_055531399.1; NZ_CP023695.1.
DR AlphaFoldDB; A0A5J6HK46; -.
DR KEGG; salw:CP975_26900; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000326553; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16915; HATPase_DpiB-CitA-like; 1.
DR CDD; cd00130; PAS; 1.
DR FunFam; 1.10.287.130:FF:000011; Sensor histidine kinase DcuS; 1.
DR FunFam; 3.30.450.20:FF:000018; Sensor histidine kinase DcuS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:QEV20689.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000326553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 402..534
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 58909 MW; 828C0BFB9D957230 CRC64;
MSPTSRVRRL RLGLPRRVFS QVLVMQLAIA AGVAVLATGL FLAPLSDQLD DQAMRRALAI
AQTTAAHPKI AEDLTSSRPT GDGPVQAEAE RIRRASGAEY VVIMNKEGIR WSHTDRTQIG
RPVSTDPSDA LAGREVMEID DGTLGRSARG KVPLRDSGGH IVGAVSVGIE YESVRARLIH
SIPGLLAYAG GALAVGAIAA YLISRRVQRQ TRDLAFSDIS ALLAEREAML HGIREGVVAL
DSGGRIRLLN DEAQRLLGLG TEVVGRPLDE ALGAGRTTDV LAGRVSGTDL LTVRGQRVLI
ANRMPTDDGG AVATLRDRTE LEQLGRELDS TRGLIDALRA QDHEHANRMH TLLGLLELEM
YEEAAEFVGE VAGAHRVTAE QITEKIRDPL LAALLVGKAT VAAERGVALS VPRETALPDR
LVDPGGLVTI VGNLVDNALD AAAGTRHARV EVAVRTEGRA VVLRVRDTGP GVPAEQRETI
FTEGWTTKEP PAHGKRGIGL ALVRRLAERQ GGSARAGEAP EGGAEFTVVL PEALTEPAFS
PTEGSTLIKG TEATP
//
