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Database: UniProt
Entry: A0A511FDI7_9CELL
LinkDB: A0A511FDI7_9CELL
Original site: A0A511FDI7_9CELL 
ID   A0A511FDI7_9CELL        Unreviewed;       807 AA.
AC   A0A511FDI7;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   08-OCT-2025, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CHO01_24350 {ECO:0000313|EMBL:GEL47319.1}, HNR08_000919
GN   {ECO:0000313|EMBL:MBB5472183.1};
OS   Cellulomonas hominis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=156981 {ECO:0000313|EMBL:GEL47319.1, ECO:0000313|Proteomes:UP000321723};
RN   [1] {ECO:0000313|EMBL:GEL47319.1, ECO:0000313|Proteomes:UP000321723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16055 {ECO:0000313|EMBL:GEL47319.1,
RC   ECO:0000313|Proteomes:UP000321723};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Cellulomonas hominis NBRC 16055.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5472183.1, ECO:0000313|Proteomes:UP000564629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9581 {ECO:0000313|EMBL:MBB5472183.1,
RC   ECO:0000313|Proteomes:UP000564629};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
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:GEL47319.1}.
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DR   EMBL; BJVQ01000035; GEL47319.1; -; Genomic_DNA.
DR   EMBL; JACHDN010000001; MBB5472183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A511FDI7; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000321723; Unassembled WGS sequence.
DR   Proteomes; UP000564629; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR   Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR051315; Bact_Chemotaxis_CheA.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 2.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 2.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 2.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:MBB5472183.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000321723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MBB5472183.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..104
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          239..486
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          488..624
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          646..777
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          130..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..157
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..185
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..204
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..221
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   807 AA;  85023 MW;  00ABD6EDC6C01F20 CRC64;
     MEDMDEIVRE FLVESHENLD QLDQDLVALE SEPGSRSLLA SVFRTIHTIK GTSGFLAFSR
     LERVAHAGEN LLVELRDGRR SMDQPTTDVL LRLVDTIREI LRAIEVDGGE GGVEVDAVIA
     AIEAIQATDP SAATEPAAEP AEAPAAEHAA QPEAAAVPPA PEPAPAPAAE DAPPALPTPR
     TPEPAAPARA IGEPAPAPAA AAAPAPAPAP TPAQTPAPAP AAVPASDEVG SLRTGAADAS
     IRVDVDLLDA LMRQVGELVL ARNQISRLAT GTDDVDLARS AQRLNLIAGE LQEGVMKTRM
     QPIEHLWSKM PRMVRDVAAA CHREVQLELS GGDTELDRSL LEAVKDPLTH LVRNAVDHGI
     EASEDRVAAG KAPKGVLSLR AYHASGQVVV EVADDGRGID PEKIGAKAVQ KGLRTTDQVA
     AMSAGDLLQL LFLPGFSTAE AVTNVSGRGV GMDVVRTKIE SIGGAVDVES TVGRGTTWRL
     RIPLTLAIMP ALTVECSGDL YAIPQVNLLE LVALDSQRSE SGIEHVHEAA VYRLRGELLP
     LVSLSSVLEV GGERPDNAVI AVVQSDHQRF GLLVDRVLNT EEIVVKPLSA RLKAVGAYAG
     ATVLGDGHVA LILDVQAIAR RALAGELDTA ARDAHANAAA ALAHEVQQVL VVGIGGGRQV
     AMPLASVARL EHVQAEQVEY VGGREVVQYR GTILPLARLD RILGAYGEQD AAELLLVVYS
     RGDRSVGLVV REIVDIVDDD SARHSDIEDA GLVGSTVLGD RVTELLDVRR AILAADPAFY
     DERAELRSTY DDLPTQVGGP ELVGATR
//
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