ID A0A366ZYN4_9ACTN Unreviewed; 825 AA.
AC A0A366ZYN4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=DQ238_07880 {ECO:0000313|EMBL:RBY80943.1};
OS Geodermatophilus sp. TF02-6.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY80943.1, ECO:0000313|Proteomes:UP000253027};
RN [1] {ECO:0000313|EMBL:RBY80943.1, ECO:0000313|Proteomes:UP000253027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-6 {ECO:0000313|EMBL:RBY80943.1,
RC ECO:0000313|Proteomes:UP000253027};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL Submitted (JUL-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:RBY80943.1}.
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DR EMBL; QOHF01000006; RBY80943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366ZYN4; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000253027; 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; cd00731; CheA_reg; 1.
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:UP000253027}.
FT DOMAIN 1..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 284..489
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 491..628
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 651..782
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 133..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
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 825 AA; 86964 MW; 391BD0F405EBA255 CRC64;
MDGLDDIVEE FLVESHENLD QLDTDLVALE QEPDSRERLS SIFRTIHTIK GTSGFLAFSR
LEEVTHVGEN MLSRLRDGEL ALTPHRTSVL LQMVDTVRAL LASIEATGGE GSVDVSAVVA
AISAAMDDAP AAAPAPAVEP APAAGDAEDA VPPAPAAGDA EDAVPEAVPE AAVDAEAAAS
EDADPEAAVP TPAVPTAEAP APPTAPAPRP EPAVEPADLH DGDAAPAADS GGRQSRRAVA
DSTIRVDVDL LDELMLLVGE LVLTRNQIVQ YVGRSNDTDL VRASQRLNLI ASELQEGVMK
TRMQPIDHIW SKLPRVVRDL GLQLQKSIRL EMEGRDTELD KTLLEAVKDP LTHLVRNSVD
HGVEAPEARR AAGKPTEGVL TLRAKHESGQ VVVEVADDGA GIDPAKVGAK AVERGLITAD
ALARMNPQDV LQLIFLPGFS TAAAVTNVSG RGVGMDVVKT NIESIGGTIE VESVPGHGTC
TRLRIPLTLA IVPALTVECA GDRYAIPQIS LQELVALDAE KAATAVEEVG GAPVYRLRGE
LLPLVRLTDV LGLTSERHDG HVVIAVLRSE GRRFGLVVDR VINTEEIVVK AVGGQLKAIG
LYSGATVLGD GTVALILDVQ ALARRALRTE TTERQESREA ALRAAASEAE RQRMLLAAIG
GGRRVAIPLD TVTRLEQVRA ESVERVGNRE VVQYRGAILP IVRLDRHLGA YGETDREVLE
VIVYTDRGRS VAIAVEEILD IVDGEAAIRS DIDDLGLLGS AVLGDKVTEL LDVRAAILAA
DPAFYSAHPS ALAHPSALAH PSALAHPSAL ATTTPDGVPG SLLEV
//
