ID E1V8E4_HALED Unreviewed; 544 AA.
AC E1V8E4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=HELO_3716 {ECO:0000313|EMBL:CBV43600.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV43600.1, ECO:0000313|Proteomes:UP000008707};
RN [1] {ECO:0000313|Proteomes:UP000008707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000313|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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; FN869568; CBV43600.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V8E4; -.
DR STRING; 768066.HELO_3716; -.
DR KEGG; hel:HELO_3716; -.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_020211_11_2_6; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_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 Pfam; PF13188; PAS_8; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:CBV43600.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:CBV43600.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..535
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 544 AA; 58748 MW; 70469627EB84B577 CRC64;
MPRPHLRLNS LIFLLVAVMV ILSLGLALWL FTAQLDEALE QSQARRVTDL AQTLADESGV
RAALLERRRQ PAVATGDAAL QSRIDGLRQR LGVDFMVVMD DRSTRLTHPE PSRIGHHFRG
GDEDRALAGE VYHSRAEGTL GTSIRGFAPV RDDQGEVIGA VAVGVTLDSL GALLADNRRD
VMVGVLLLMI VGALGARWLA RYIKRVLLGL EPYQITRLVE ERQAMLASVH EGILAVDREA
RITLANPTAR QLLAGAGLGS PPLGEAVADY LPHSGLPEVL AGDGEKLDRE LDLNGQVVLA
NRLPIHHRGQ VIGAIATFRD KSEVNALAEQ LTGVSRYAEA LRATTHEFKN QRHVMLGLAQ
MGDLDSLRGY LGELVDHHVT QGVVLASDIE DPVLAGFLLG KCSEARERNL HLEVLLESSL
PTPAESASAH TLVTVLGNLL ENAFDAVEGR DERCVTLTLS WDEDLLDVHV QDTGDGIAPR
VRERLFEPGV STKGVRRGLG LSAVRERVEA CGGSLAVYSE TGRGALFEVE LPYPVASQSG
EGEG
//
