ID A0A1M3FXF2_9SPHI Unreviewed; 473 AA.
AC A0A1M3FXF2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BGO54_16410 {ECO:0000313|EMBL:OJW32004.1};
OS Sphingobacteriales bacterium 46-32.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW32004.1, ECO:0000313|Proteomes:UP000184358};
RN [1] {ECO:0000313|EMBL:OJW32004.1, ECO:0000313|Proteomes:UP000184358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46-32 {ECO:0000313|EMBL:OJW32004.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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};
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:OJW32004.1}.
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DR EMBL; MKTY01000020; OJW32004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3FXF2; -.
DR STRING; 1895839.BGO54_16410; -.
DR Proteomes; UP000184358; 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 CDD; cd19410; HK9-like_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
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; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 473 AA; 54159 MW; FD8DC0A79776E7F1 CRC64;
MPLSRVKIRW GYLIALILML VSYTMIFMII RRLVRETGWV THSYMIINKL ESLKSEITDA
ETGVRGYLIT NDYVFLKPYN SGIRNTLPLY EQLLSLSKDN PRYKSRLDTL GVLIRRRLAS
LSSTVRQYQQ QGFKLNEKLL ANRDENRLIM DSVRLLITQL QDEENTLVTH RDKNLSGIFR
NTANSTVVSL VIALITISYS VIIYNRENKA KEKAISNARN YSLQLEERVV ELDRVNNELQ
ELKSIEKFAA TGRIARTMAH EVRNPLTNIS LASEQLKEIT GQQEEADMLL DMIGRNVNRI
NQLVSDLLNS TRFAQLEYTH ENINNLIDET LELAKDRIDL NHIQVSKSYA RDLCTVYVDK
EKIKLAFLNI IVNAIEAMER TSGQLEIRTR KVGPKCQVEI HDNGIGMDEE TIQRLFEPYF
TGKLSGNGLG LTNTQNIILN HKGNIQVKSK VGQGSVFIVT LALNDETPSR REL
//
