ID E1X3P3_HALMS Unreviewed; 485 AA.
AC E1X3P3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BMS_2166 {ECO:0000313|EMBL:CBW26972.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW26972.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
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; FQ312005; CBW26972.1; -; Genomic_DNA.
DR RefSeq; WP_014244750.1; NC_016620.1.
DR AlphaFoldDB; E1X3P3; -.
DR STRING; 862908.BMS_2166; -.
DR KEGG; bmx:BMS_2166; -.
DR PATRIC; fig|862908.3.peg.2060; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_562325_0_0_7; -.
DR Proteomes; UP000008963; 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; IPR033414; Sensor_dom.
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; PF17149; CHASE5; 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 Reference proteome {ECO:0000313|Proteomes:UP000008963};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..485
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 485 AA; 56025 MW; 85C0DD0B2C2EB031 CRC64;
MFKEIETKKF TSLRKKLMLA ILFASSFITL ITTGLQYYIE YQRDITYLSQ TIKHIGSSNT
SSLSRSLWNL DDMQIQVQMD AILKLRDLIG VAIYDEDGQV YYQNTDHEFK TLEKFETRFK
LDLNESNYTH KLGELVIWAT RDHITENLIS RLTTFFLAQL VKTFMVIFVM LYLFRIFITK
HLDYIVRFLQ FSDFNSLKIE RISLAKNTKS IDELDYVADS INLMLERVER ANLETNDKFL
RQEKEIQLQK AASINSARLA SLGEMAANIA HEINNPLTVL SFSGKKILHL LRADELDRDR
IKHFASMINR TVDRMTKTIT SLKRLSRDTS TDQFKDVVIY DMIERVLDLC QMSLNEKGIE
LSTEFIGFDF STKIKCQEVK VSQVIINLLN NARDEVKNME KPWIKLLVIK SDELISFSVI
DCGTGIAGEV QEKMFEPFFT TKDIGEGTGL GLSISSSTAK EHKGRLFIDN NSENTKITLE
FPLDL
//
