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Database: UniProt
Entry: F3Z6Y9_9ACTN
LinkDB: F3Z6Y9_9ACTN
Original site: F3Z6Y9_9ACTN 
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};
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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
//
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