ID A0A0F7NE39_9ACTN Unreviewed; 721 AA.
AC A0A0F7NE39;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AA958_25155 {ECO:0000313|EMBL:AKH84952.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH84952.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH84952.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH84952.1,
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; AKH84952.1; -; Genomic_DNA.
DR RefSeq; WP_047018203.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7NE39; -.
DR STRING; 444103.AA958_25155; -.
DR KEGG; strc:AA958_25155; -.
DR PATRIC; fig|444103.5.peg.5301; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000034283; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 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; IPR003594; HATPase_C.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:AKH84952.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transferase {ECO:0000313|EMBL:AKH84952.1};
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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..544
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 542..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 73885 MW; E2DFA59D3FA62EA9 CRC64;
MRLPRPRSLA GQLFAMQVVL VTLMVAGAAI FMYVTAHDRA EEAAARQAES TARSVAAAPG
VAEAITGGGT PSGVLQPYTE RARRDTAVTF ITIMAPDGTR YTHPNPDVIG EAFLGHTARA
LRGETFTETY TGTLGPSLRV VTPVRADDGR IVGLVSAGIT VKTISDEVRR QLMPVLYVAA
GALALAGLAT YLINARLRRH THGMNAGELS RLHDYHQATL HAVREGLLML DGTGRIALVN
DGARELLGMG PGGEVVGRPV ADLGLPAPLT EALLSPGPRV DEVHLTRDRT VVVNTSPVTG
GEHRGTVVTL RDVTELQTLT GELDSARGFA EALRSQAHES ANRLHAVVSL IELGRTEQAV
EFATAELELA QTLTDRVTGA VTEPVLAALL LGKAAQANEQ GVELVLSPDS RIDDGVLPPT
LPPRDLVTVL GNLIDNAVDA AAEGARTRTA SGTRDTAQPQ VRVTALAADG ELLLRVADDG
PGVDPSRAEE VFARGWTTKR AGPAGRGLGL ALVRQAARRH GGEATLTGAE AGGAEFTVRL
PLGPLGAPAP ETGWPQKGTA KAAAEPLSGP GPEAGDPRGG PAPGAGAAPG EPVTAAPAAG
GGPAAETAAQ PRDPADGGSA ASAPRVPAAR NPADDGPRRH RPTGPAGSPT APRSPVPGTP
TAQPDPGGSA SGPHRPACPS TPTAPARPAN PPDSPARSAP RTRAGHPCPR RPADADRPGD
R
//
