ID F3Z6Y9_9ACTN Unreviewed; 1070 AA.
AC F3Z6Y9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=STTU_1956 {ECO:0000313|EMBL:EGJ74744.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ74744.1};
RN [1] {ECO:0000313|EMBL:EGJ74744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ74744.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001165; EGJ74744.1; -; Genomic_DNA.
DR AlphaFoldDB; F3Z6Y9; -.
DR HOGENOM; CLU_002554_3_0_11; -.
DR Proteomes; UP000003955; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR013587; Nitrate/nitrite_sensing.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08376; NIT; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGJ74744.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1070
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003303436"
FT DOMAIN 353..409
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 562..672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 691..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 425..452
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 886..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 110344 MW; 47C154B0F8693927 CRC64;
MPPPAPPAGR RKRVRSRLVI AVAVVAAAVA GAGAPALADA TDRAHEAQRL VDDAGVAQQS
TALAQALADE RDEVTSYIAS GRPRGDGLSE QRSARVDRGV QELEAADIPK GLRDQLDAIS
GVRRQALTGK GTALAAHTSY SRIIEHLHAR VALLADALPQ DAAEAPHALV DLDTAVTEAG
AVRGLLLAAL AVPRPTGTET RVDPMTGIAT TVPVSDPAGD RQRDALSRAA HEAQIRSEAA
LAAFRATARE ADLSAYTSTV TGADVNNAEK YLARLTDEPT LDDGDLGLKT SKVSAALGAR
IELMRSADAA LAVDRSHRTE ALRDDEVQSL ELRVVLVGVL LLAAAGVGMA TARSLTRPLA
ALRLGAKRLA EADDPAAEEP VRFTGRNDEF AQVVHSVNVL HAHAVSLHER LGTLEGDRKH
LVGQRQSVAA DRDRLRAELA GVQEQLDLAK GSINGTFVNL ALRTLGLVER QLGVIENLEE
REQDPDRLAT LFKLDHLATV MRRHSENLLV LAGAEHGVQN PNPVPLVDVL RAAVSEIERY
ERVRIAALPP HAHIAGFSAD DLSHLVAELL ENATSFSPPD AQVEVSAWLL ENGEVMLSVQ
DEGIGMSAAR LDEVNELLTS FQPGDTLGEE QEGLGLGLYV VARLSSRHGI RVRLREQKQG
GIAAVVVLPP PILATPAAGV VTPHAGGHLA GPAPTVALPG SEAEANSNEL PGREAAEPSA
SGTGTAASGT GQEAAAAGTG EEAPAAGTGQ DAPAAGTEQD APAAGTEQRN PVAEDRVTPA
APGPDPLIAA AEASVAAAHG TEDANPAGEA APAASTPAED VPAERPAPAK PAASGPGVAP
APTVEPSSET TMILHLPPAP GGEGTTGTDG TPPARDDAPA PVPEQRRPTT ERPPVPEEAA
PAPAEPVAPQ ELTAPQEPPA AAASPASPAS PYAIGPDAHA RIPDTAEAEA AEAERVESWD
RVTDKGLPKR TPKISAPAPA PRTATPGVDA EALRRRLGGF HQGATQGRKD VEAALAEESG
SLTLPGTEDE EPARGSASAR PGSTRPPAAP TTADAREVSA EGDSAEEERR
//