ID E1WZZ1_HALMS Unreviewed; 551 AA.
AC E1WZZ1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BMS_3173 {ECO:0000313|EMBL:CBW27927.1};
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:CBW27927.1, 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; CBW27927.1; -; Genomic_DNA.
DR RefSeq; WP_014245697.1; NC_016620.1.
DR AlphaFoldDB; E1WZZ1; -.
DR STRING; 862908.BMS_3173; -.
DR KEGG; bmx:BMS_3173; -.
DR PATRIC; fig|862908.3.peg.3033; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_494147_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; 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; 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; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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 Kinase {ECO:0000313|EMBL:CBW27927.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008963};
KW Transferase {ECO:0000313|EMBL:CBW27927.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..447
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 551 AA; 62960 MW; 54E3153480462F23 CRC64;
MKINLSLSRA VSIPLLLLNI IFSVVLSFYL YTAFERINND NIKKLYNENL NLFSSLVSQD
IIMGQYASVE KKCNQYFDQN SVNYIQILTD EFIICKSGTE VSNGEVLKKT LFFDEQKKEV
LAEIVLGYHV KKGFISETGP LLVFLGISFV ILTFVTNHYL IRIVIRPLQK VTKSLSGVVN
VEQAKEDIYY RDQILQIDEL KSLFENRNEL LFQLKSYQDE QIKNAENKIV VEVARQVAHD
IRSPLAALDM AVNELKGLES GRFNLIKTAL ERIRSIANNM HQKTRELVFS ESEVSLSKFI
VHDLLVDIIE EKKLEFMSLT DLEIEYEHNN FVETELLLGD SSEYKRVFSN IINNSVEALK
EAKGKVSIKL DFDERFLYLN ISDSGQGISE DKMSKIFEKN YTSGKDNGTG LGLHYAREII
SKSGGNIFVS SVVDEGTQLS ISIPRLKKKY VLIDDDELIR LTWESAAKSK SVEFYSFSSC
IDFEKSLDSL GSDFTLYIDS SLSDDVKGEI KAKEYFELGI SEIYLTTGFE KSSFEQMSWI
KRIVPKDPPW V
//
