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Database: UniProt
Entry: A0A372M214_9ACTN
LinkDB: A0A372M214_9ACTN
Original site: A0A372M214_9ACTN 
ID   A0A372M214_9ACTN        Unreviewed;       571 AA.
AC   A0A372M214;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DY218_22485 {ECO:0000313|EMBL:RFU84513.1};
OS   Streptomyces triticagri.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU84513.1, ECO:0000313|Proteomes:UP000263094};
RN   [1] {ECO:0000313|EMBL:RFU84513.1, ECO:0000313|Proteomes:UP000263094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU84513.1,
RC   ECO:0000313|Proteomes:UP000263094};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of Actinobacteria from
RT   wheat.";
RL   Submitted (AUG-2018) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RFU84513.1}.
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DR   EMBL; QUAK01000120; RFU84513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372M214; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000263094; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; 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; IPR035965; PAS-like_dom_sf.
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; 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; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RFU84513.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          399..531
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          529..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  60479 MW;  12AA1394FB8C5D59 CRC64;
     MSAGRRVRIG MPKRVFSQVL LMQLSIAAGV AVLATGLFLA PLSEQLDDQA MRRALAIAQT
     TAAQPGIAAD LRDTAPAVDG PVQQEAERVR RATGAEYIVV VNTRGIRWSH TSPDEIGRMV
     STDPGAALAG RDVMEIDDGT LGRSARGKVP LRDSSGKIVG AVSVGIEYDS VRDRLIHTIP
     GLFAYAGGAL AVGALAAYLI SRRVRGQTRD LAFSDISALL AEREAMLHGI REGVVALDRG
     GRVRLLNDEA QRLLKVGPEV IGEPLDTAFG PGRTTDVLAG RVTGTDLVTV RGQRVLVSNR
     MPTDDGGAVV TLRDRTELER LGRELDSTRG LIEALRAQDH EHANHLHTLL GLLELEMYDE
     AVEFVGETVG THRATAEQIT EKVGDPLLAA LLVGKATVAA ERGVALRVSD DTRLPDHLVD
     PQGLVTMVGN LVDNALDASM GTDHARVEVA LHTEGRSVRL RVRDSGPGVP PERQELIFTE
     GWSTKEPPAH GRRGLGLPLV RRLAERQGGT ARCSNTPGAG AEFTVVLPEA LAPPARDTAA
     GTGAGPETEA RPGAGARPGS DARPGTVEEA R
//
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