ID A0A1G9ZZU1_9ACTN Unreviewed; 780 AA.
AC A0A1G9ZZU1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05660642_04450 {ECO:0000313|EMBL:SDN26695.1};
OS Geodermatophilus siccatus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137991 {ECO:0000313|EMBL:SDN26695.1, ECO:0000313|Proteomes:UP000198680};
RN [1] {ECO:0000313|EMBL:SDN26695.1, ECO:0000313|Proteomes:UP000198680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45419 {ECO:0000313|EMBL:SDN26695.1,
RC ECO:0000313|Proteomes:UP000198680};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNHE01000015; SDN26695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ZZU1; -.
DR STRING; 1137991.SAMN05660642_04450; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000198680; 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 Kinase {ECO:0000313|EMBL:SDN26695.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:SDN26695.1}.
FT DOMAIN 1..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 259..464
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 466..603
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 628..759
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 187..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 780 AA; 82702 MW; BB7E1E2957773AB7 CRC64;
MDGLDDIVEE FLVESHENLD QLDSDLVALE QEPDSRDRLS SIFRTIHTIK GTSGFLAFHR
LEEVTHVGEN MLSRLRDGAL ELTPQRTSVL LRMVDTVRSL LASIEATGGE GSVDVSAVVA
EISAAMEDTP AAPAPAAEPV PAVAEPAMAV AEAVEAPAVQ APVEPAAVVG APAPVAEAPA
VPAVPAPRPA PAAEVAPEPE GVADGGSGQA RRGVADSTIR VDVDLLDELM LLVGELVLTR
NQIVQYVGRS NDTDLVRASQ RLNLIASELQ EGVMKTRMQP IDHIWSKLPR VVRDLGLQLQ
KSIRLDMEGR DTELDKTLLE AVKDPLTHLV RNSVDHGVED AETRLRVGKP AEGVLTLRAK
HESGQVVVEV ADDGAGIDPA RVGAKAVERG LITQEALGRM NPQDVLQLIF LPGFSTAAKV
TNVSGRGVGM DVVKTNIESI GGTIEVESVP GKGTCTRLRI PLTLAIVPAL TVECAGDRYA
IPQISLQELV SLDAEKAANA VEEVGGAPVY RLRGELLPLV RLTDVLGLTS DRHDGHVVIA
VLRSEGRRFG LVVDRVINTE EIVVKAVGGQ LKAIGLYSGA TVLGDGTVAL ILDVQALARR
ALRTETSERG QEAAREAAAA AAAGDTERQR MLLAAIGGGR RVAIPLDTVT RLEQVRTESV
EKVGNREVVQ YRGAILPIVR LDRHLGAYGE SDREVLEVIV YSDHGRSVAI VVEEILDIVD
GEAAVRSDID DMGLLGSAVL GDKVTELLDV RAAILAADPA FYSSPMTPDG VPASLLEASL
//
