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Database: UniProt
Entry: W9GRS2_9MICO
LinkDB: W9GRS2_9MICO
Original site: W9GRS2_9MICO 
ID   W9GRS2_9MICO            Unreviewed;       407 AA.
AC   W9GRS2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=N864_23645 {ECO:0000313|EMBL:EWT07757.1};
OS   Intrasporangium chromatireducens Q5-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT07757.1, ECO:0000313|Proteomes:UP000019494};
RN   [1] {ECO:0000313|Proteomes:UP000019494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) 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:EWT07757.1}.
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DR   EMBL; AWQS01000005; EWT07757.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9GRS2; -.
DR   PATRIC; fig|584657.3.peg.290; -.
DR   Proteomes; UP000019494; 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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EWT07757.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {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        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..142
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          150..367
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          345..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  43460 MW;  DDB2E40D08AC8832 CRC64;
     MWGAQGLASR FMAALLAVLV ASIITAALVA AVLGPPIFHE HLIEAGHAAD SPEIVHIEEA
     YRDSSLTSLG VALLVAVACA SVVAWYLSRR LQIPLGALTR AAREVSRGHY DRRVAITGAS
     RELDTLAEAF NTMATRLEQV EDTRRQLLAD LAHEMRTPVS TVRAYSEGLQ EGVVAWDETV
     AAVLRDQSDR LGRLAEDLED VSRAEEGRIP LNLRPSRVGD LVWVAADAAR AAYQLKGVNL
     VVDVDRAAGL RVDVDVQRFG QIIANLLGNA LRHTPEGGTV LVVAFRDRAE VVFRVTDNGD
     GIPAEQLPHV FERFYRGDTA RDRTQGGAGI GLTISRALAD ALGGSLTASS PGPGQGSTFT
     MTLPTTSTGR GVRHTTLATP EAAAIIEATH LGLRRSTAPR SAPQEMP
//
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