ID A0A2T9XTI4_9CELL Unreviewed; 821 AA.
AC A0A2T9XTI4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DDP54_10775 {ECO:0000313|EMBL:PVU83401.1};
OS Cellulomonas sp. WB94.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2173174 {ECO:0000313|EMBL:PVU83401.1, ECO:0000313|Proteomes:UP000245142};
RN [1] {ECO:0000313|EMBL:PVU83401.1, ECO:0000313|Proteomes:UP000245142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB94 {ECO:0000313|EMBL:PVU83401.1,
RC ECO:0000313|Proteomes:UP000245142};
RA Anderson E., Ishii S., Jang J.;
RT "Cellulomonas - woodchip bioreactor.";
RL Submitted (APR-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:PVU83401.1}.
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DR EMBL; QEES01000002; PVU83401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9XTI4; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000245142; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 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; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000245142}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 226..487
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 489..636
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 656..789
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 146..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 821 AA; 86660 MW; 0ECB397A81116D84 CRC64;
MEDMDEIVRE FLVESHENLD QLDQDLVALE STPGSRELLS SIFRTIHTIK GTSGFLAFSR
LEQVTHVGES LLVDLRDGRR SMDQSTTDVL LRLVDIVRDI LAAIDLDGTE GEVVVDEVMA
AIVRVQEQVP GEVAVEPAVT PAPVAEVPAQ RSATPSTTPA PVATEVSAEP VDAAEPELDD
EPEVEPVPEP VAPKAASATK VQSAAAVVPS PRASEPAAAP APAAAAAPEE AAAPRTSADS
SIRVDVGLLD ALMRQVGELV LARNQISLLA SGADDVELSR SAQRLNLIAG ELQEGVMKTR
MQPIDHVWSK MPRVVRDLSA QCEREVALEM IGGDTELDRG LLEAVKDPLT HLVRNAVDHG
IEPPAERVAA GKPAKGVLTL RAFHEGGQVV VEVADDGRGI DDEKVAAKAL QRGLRTADEL
AAMGPSEIVQ LLFLPGFSLA DTVTNVSGRG VGMDVVRTKI EAIGGTVDVE TAVGQGTAWR
LRIPLTLAIM PALTVECAGD LYAVPQVNLL ELVALDAQRT DSAIEYVQAA PVYRLRGELL
PLVSLAAVLR VDGPFGAAAV AGGPARSGNQ VIAVVQADQQ RFGLLVDRVL NTEEIVVKPL
SSRLKTLGVY AGATVLGDGR VALILDVQTI SRRALTSDVD LRRARAAAEV TKTVALEQVL
VVGIGGDRRV AMPLASVARL EHVRLSEVEL VGGREVVQYR GTILPLIRLD RLLGGYGSMA
DQSDELLLVV YLEAGRSVAF VVAEILDIVD DDGSQHSDIE DAGLVGSTVI DGHVTELLDV
RGAVLAADPA FYDVRADASA AVPDTGSAGP VSRYDLVGAV R
//
