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Database: UniProt
Entry: C9Z0J4_STRSW
LinkDB: C9Z0J4_STRSW
Original site: C9Z0J4_STRSW 
ID   C9Z0J4_STRSW            Unreviewed;       575 AA.
AC   C9Z0J4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=SCAB_24351 {ECO:0000313|EMBL:CBG69547.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69547.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG69547.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG69547.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FN554889; CBG69547.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9Z0J4; -.
DR   STRING; 680198.SCAB_24351; -.
DR   KEGG; scb:SCAB_24351; -.
DR   eggNOG; COG3290; Bacteria.
DR   HOGENOM; CLU_020211_11_1_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          410..521
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          527..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  60762 MW;  5B06F0A8A08CD936 CRC64;
     MPRRVFSQVL LMQVAIAAGV AVLATGLFLA PLSQQLDDQA MRRALAIAQT TAAQPQMARD
     LVSTRPSVTG PVQVEAERIR KASGAEYVVV LDRRGVRWSH PDPTEIGGLV STDPRRALAG
     KEVMEIDSGT LGRSARGKVP LRDADGRIVG AVSVGIEYDS VRDRLFHAIP GLLAYAGGAM
     AVGALAAYLI SRRVHRQTRD LAFSDIAGLL AEREAMLHGI REGVVALDRA GRVRLLNDEA
     RRLLGIGDEA VGSSLDDALG AGRTTDVLAG RVTGTDLLTV RGQRVLVANR MPTDDGGAVA
     TLRDRTELEQ LGRELDSTRG LTDALRAQDH EHANRMHTLL GLLELEMYDE AVEFVGEVVG
     EHRATAEQVT EKIHDPLLAA VLVGKATVAA ERGVALSIAD GTMLPDRLID PRGLVTVVGN
     LVDNALDAVA GTPCARVEVD LRTEGRTAVL RVRDTGPGVP PDKRELIFTE GWSTKTPPAH
     RERGIGLSLV RRLAERQGGT ARVTEAAGGG AEFTVVLPDA LAEHGLVTPA PSAAPAPVAP
     EDGPARRDGP GAGHDGRPGS AREPEAAGTA DKEPR
//
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