ID A0A1W1V6R6_9BACT Unreviewed; 510 AA.
AC A0A1W1V6R6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN00120144_3462 {ECO:0000313|EMBL:SMB88694.1};
OS Hymenobacter roseosalivarius DSM 11622.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=645990 {ECO:0000313|EMBL:SMB88694.1, ECO:0000313|Proteomes:UP000192266};
RN [1] {ECO:0000313|EMBL:SMB88694.1, ECO:0000313|Proteomes:UP000192266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11622 {ECO:0000313|EMBL:SMB88694.1,
RC ECO:0000313|Proteomes:UP000192266};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWWW01000051; SMB88694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1V6R6; -.
DR STRING; 645990.SAMN00120144_3462; -.
DR OrthoDB; 9766459at2; -.
DR Proteomes; UP000192266; 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 CDD; cd19410; HK9-like_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SMB88694.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000192266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 286..496
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 510 AA; 58170 MW; C33BB872C2C7BD4B CRC64;
MRLNLNTKIR LGFGIALIVL LLTSLLAYLS IQQVAYYTNR VEHTYRVLQH TTNLRSQMRD
AQGAIRGYLL LGDKSYLNNY DDLLNGVRDD YEGLRHLTID NPDHQRRLDT LGSFMAQEVL
LLDAWRQRPP SPYAARDLVR GDRRLLEQIR AIITRIKDSE DLLLHQRTRY RDIWERTAPL
AIIGSAVLAI LIVLRLFSRI VRELKEKERL QAELAAVNRD TTQRIQLIEN LAEQVVLGDY
KVKIRDKEQD SLGKLAGSLN RMTQTLDQNF EALNKRNLEL DQFAYVTSHD LKAPLRGIGT
LVKWMEDELS HELSAQMREY LAMLKGRLTR LDDLINGLLA YARAGRTQPV PEEVEVRELV
AEVAEMVVPQ EFTLDLPPSL PPFLTDRLSL QQVFTNLLSN AIKHHHSGQG HLIIGAQELK
KEYEFSVTDD GPGIAPEYHE KIFQIFQTLR DRNTAESTGI GLSIVRKIIE EHKGSIRVQS
VPGQGATFVF TWPKALMPVS LVTTPVTIPL
//
