ID A0A3E1NDC7_9BACT Unreviewed; 722 AA.
AC A0A3E1NDC7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DXN05_23050 {ECO:0000313|EMBL:RFM25841.1};
OS Deminuibacter soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Deminuibacter.
OX NCBI_TaxID=2291815 {ECO:0000313|EMBL:RFM25841.1, ECO:0000313|Proteomes:UP000261284};
RN [1] {ECO:0000313|EMBL:RFM25841.1, ECO:0000313|Proteomes:UP000261284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K23C18032701 {ECO:0000313|EMBL:RFM25841.1,
RC ECO:0000313|Proteomes:UP000261284};
RA Wang C.;
RT "Chitinophagaceae sp. K23C18032701, a novel bacterium isolated from forest
RT soil.";
RL Submitted (AUG-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:RFM25841.1}.
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DR EMBL; QTJU01000014; RFM25841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1NDC7; -.
DR OrthoDB; 9806995at2; -.
DR Proteomes; UP000261284; Unassembled WGS sequence.
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; 2.60.40.2380; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 467..719
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 391..458
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 722 AA; 80685 MW; 53C479206C1432FA CRC64;
MRNRKQITLR LIYLFVALVL GGNSIVKAQA PVITNEAGLT CRLSVLEDKT AQLDADAVKN
AAFTPLQSNA VNYGLSNSAY WIKIDVTNPS PQKEFLFGIR NGTITEATLY VKDSTGHYRQ
TGAGGSTIPV SLKIFRTQYP VFDMYVPQGN SVTYLLRIKS DDVLDLPFQL NTESKIHDSI
SADLYIFGIY LGIILIMFLY NLFIYLSVKD SNYLYYVLYI LTIGITQASL KGFSTRFFWP
DSPWLISQAH NVSIALSGIG SLLFVLQFLH VKRFSKRVFY FFLLLMAVYV AGIVINLSGN
YMLSQQILQQ NATVVALSIM SCGIWIMRKG VREAVYFNIS WFFFLAGVII YILKDAGILP
FNDFTSNSIL IGSGLEVSLL SFALADKINT YKKEKEESQA MSLRISQLNE QLVREQNVVL
ERKVTERTEA LQQANAQLSE TLQDLKEAQM QLVEAEKMAS LGQLTAGIAH EINNPINFVK
SNIKPLRLDI RDLFEVIGEY DALHSKDIND IPAALKKIDA LKTEIDMGLV SAEITNLIKG
IEDGAERTAE IVRGLRTFSR LDESELKLVN VHDGIESTLV LLRNNIPHQV SIIKKFEAEG
NIECYPGKLN QVFMNILNNS VQAINAKKDS MENEFISILT RDIADNCIEI SIKDSGIGMT
EEVKQKIFEP FFTTKEVGEG TGLGMAIVFK IIGSHHGKIN IVSEPGKGAE FIITLPYLQS
II
//
