ID A0A0N1DYH6_9FLAO Unreviewed; 459 AA.
AC A0A0N1DYH6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMQ68_19460 {ECO:0000313|EMBL:KPH11574.1};
OS Chryseobacterium sp. ERMR1:04.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1705393 {ECO:0000313|EMBL:KPH11574.1, ECO:0000313|Proteomes:UP000037945};
RN [1] {ECO:0000313|EMBL:KPH11574.1, ECO:0000313|Proteomes:UP000037945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:04 {ECO:0000313|EMBL:KPH11574.1,
RC ECO:0000313|Proteomes:UP000037945};
RX PubMed=26543128;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Genome Assembly of Chryseobacterium polytrichastri ERMR1:04, a
RT Psychrotolerant Bacterium with Cold Active Proteases, Isolated from East
RT Rathong Glacier in India.";
RL Genome Announc. 3:e01305-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000037945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:04 {ECO:0000313|Proteomes:UP000037945};
RA Swarnkar M.K., Kumar R., Singh A.K., Singh D.;
RT "Genome Sequencing of Chryseobacterium sp. ERMR1:04 isolated from Glacier
RT Moraine Ridge soil.";
RL Submitted (AUG-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};
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:KPH11574.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIRF01000008; KPH11574.1; -; Genomic_DNA.
DR RefSeq; WP_054512258.1; NZ_LIRF01000008.1.
DR AlphaFoldDB; A0A0N1DYH6; -.
DR STRING; 1705393.AMQ68_19460; -.
DR PATRIC; fig|1705393.3.peg.4094; -.
DR OrthoDB; 594725at2; -.
DR Proteomes; UP000037945; 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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..230
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 238..457
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 257..284
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 459 AA; 53328 MW; 387E0CE7A99EF28B CRC64;
MKIATRTALN YAILTAGILF LFAYVLYFVS EKNREDEFND RLGYKITWRS EFIFDAKIDD
SKIRELHERN KKLLNEADIS VYDSNKKLIF TDIQPSSKNQ YYLDQLIKTK KNRITWQRGD
RQYMAFKYEF NNENFYIIGS ATDVTGKAHI EEFKKDVIII YIISIVIIFI IGFLFSYYTL
KPLKDIILQI RDISEHNLNK RLVVPKAKDE IYELTETFNS TFNRLEKSFN NHKQFVTTIS
HEFRTPLSTL IAELELAKEL NITLEDYKIS IDNALQDANQ ASQLSSALLD FARASYDVSQ
ISFVDLRLDE VLADAKVALL QKNSEYRIGI HYMDNLADKD ESNYDFHGNP YLLQIAFLNL
MENACKYSSD KNCSVEIEVQ NNNLEIRFID HGIGISEADQ LKIFDLFYRG NNKNYDKGNG
IGLSIVKRII EMHLGNLSLQ SEPSKGSTFT IQFVSRNRL
//
