ID A0A0U4C8W0_9BACT Unreviewed; 502 AA.
AC A0A0U4C8W0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AUC43_17570 {ECO:0000313|EMBL:ALW86728.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW86728.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW86728.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW86728.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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; CP013909; ALW86728.1; -; Genomic_DNA.
DR RefSeq; WP_068196697.1; NZ_CP013909.1.
DR AlphaFoldDB; A0A0U4C8W0; -.
DR STRING; 1411621.AUC43_17570; -.
DR KEGG; hyg:AUC43_17570; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000059542; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..502
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 502 AA; 55622 MW; F198CBDB5067B8D3 CRC64;
MDYLQLVPAA WRLRFPDATE REFIDYYNVT TINAIRISLA VGVILYAAFG LLDLNSLPVT
TSTAWFYRFS VGCPAIFIAL LFSYITPLRG LLQVVMTVMC IVAGLALVLI VRQSQPTELA
YDHYYVGVII IMMFTGSWVR LRFWHALAAH TVIIGAYFIL VSHARHLAVD RHLIVNNTVF
LLAAYFVASL TGYIFEVDSR IGFLQWKTIE AEKNTSNLQR EEITVQAQQL AETIGVLKDT
QAQLVQREKM AALGELTAGV AHEIQNPLNF VKNFAEVSRE MLEEMQQSLA NEHLTEPGTA
TVQALLRDLG NMQQKIGQHS QRADAIVKGM LEHSRSTGGN RQPTDLNRLA EEALRLSYHN
RQLQEPAFTA NLATDFDPHV GLVSVASTDI QRVLLNLLGN AFYSVSHKKQ RLGAAFTPQV
KVATKRRGKG VEIRVRDNGA GMSKEVLQKL FQPFFTTKPP GEGTGLGLSI SHDIITSGHG
GAISATSQSG EYAEFCITLP AM
//
