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Database: UniProt
Entry: A0A0F0KTX8_9MICO
LinkDB: A0A0F0KTX8_9MICO
Original site: A0A0F0KTX8_9MICO 
ID   A0A0F0KTX8_9MICO        Unreviewed;       531 AA.
AC   A0A0F0KTX8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=phoR {ECO:0000313|EMBL:KJL23944.1};
GN   ORFNames=RL72_01896 {ECO:0000313|EMBL:KJL23944.1};
OS   Microbacterium azadirachtae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL23944.1, ECO:0000313|Proteomes:UP000033448};
RN   [1] {ECO:0000313|EMBL:KJL23944.1, ECO:0000313|Proteomes:UP000033448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL23944.1,
RC   ECO:0000313|Proteomes:UP000033448};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-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};
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:KJL23944.1}.
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DR   EMBL; JYIT01000075; KJL23944.1; -; Genomic_DNA.
DR   RefSeq; WP_045250576.1; NZ_JYIT01000075.1.
DR   AlphaFoldDB; A0A0F0KTX8; -.
DR   PATRIC; fig|582680.7.peg.1945; -.
DR   OrthoDB; 9757990at2; -.
DR   Proteomes; UP000033448; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 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; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033448};
KW   Transferase {ECO:0000313|EMBL:KJL23944.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          180..222
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          312..526
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   531 AA;  57292 MW;  B6651828BC655A3A CRC64;
     MSRRASIWRW QLIFVSTTVA IAVLVAALKP TVFATPLFTA GLLLSLVATI VVLVLPWDRI
     PPAGILAVPM VDIVAIGLTT QAPDIRLGFL WVIPITWIAT YYSMIAVFGG IALITAFLFT
     IANQTGLFSD VVLRVLITAF ALGFLGTTIR IGVKRSRASS RLLRRRSEQI DRIARRAETH
     ERRVTQIIDA LDTALVALGD DGVILKMNDA YRRLYGVDAD GIALPAPAVE YDDREGEPVP
     VHRTVLARAS RGEQLDGERV WLYDADGVWR ALEVSTRPMA SDADQGAVNL VRIDDVTAAL
     AAAEERRLMS AILTHELRNP LTAIVGHVDL LLERDDLPAR AADQLTVVAG AAERMQDLVT
     TALDASRPAR RVLSEPVDLH ALVRASVSSF LPTATAGRIR VDVTGASALL IYGDAFRLRQ
     VIDNLLSNAV KYTAAGGSIV VSLDVADDAL AELVVADTGS GMAPADVERL FEPYFRGEQA
     AHGGVPGTGL GLVTVRDIVT AHGGTVDVHS RLGEGTRMRV RLPRRPERND A
//
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