ID A0A1W5ZV98_9BACI Unreviewed; 593 AA.
AC A0A1W5ZV98;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HM131_10330 {ECO:0000313|EMBL:ARI77210.1};
OS Halobacillus mangrovi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=402384 {ECO:0000313|EMBL:ARI77210.1, ECO:0000313|Proteomes:UP000192527};
RN [1] {ECO:0000313|EMBL:ARI77210.1, ECO:0000313|Proteomes:UP000192527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTB 131 {ECO:0000313|EMBL:ARI77210.1,
RC ECO:0000313|Proteomes:UP000192527};
RA Lee S.-J., Park M.-K., Kim J.-Y., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F.,
RA Lee D.-W.;
RT "The whole genome sequencing and assembly of Halobacillus mangrovi
RT strain.";
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP020772; ARI77210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5ZV98; -.
DR STRING; 402384.HM131_10330; -.
DR KEGG; hmn:HM131_10330; -.
DR Proteomes; UP000192527; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR041328; HisK_sensor.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF18698; HisK_sensor; 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 SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ARI77210.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 189..241
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 366..588
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 593 AA; 67176 MW; B2411A56D517EFFC CRC64;
MFWRSVVGKL WFTILLLVCF VLFILTILLL EFFQNYHILE AERHLLQTAN KISDVEERYE
DRELMLSTTN LVKDSASRAV IAWDERDILI ADSETDELPE LGYEWFASDQ ELSSVINKGN
EVKKVADLET SETGVMVVGT PLANGEGAVF VYQSLDTIEE TSEQTTKIIF LGAGIAIVLT
TIFAFFLSTR ITSPLIKMRE GALELAKGEF NNKVPILTHD EIGELAMAFN RMGRQLKYHI
NALNQEKEQL SGILRSMADG VITINRTGEI LVTNPPATQY LDAYAFEHKE DMSDAQTLPE
PLTALFKKVI TNEEESMTEV TLQGRSWVII MTPLYDKSTV RGAVAVLRDM TEERRLNKLR
KDFIANVSHE LRTPISMLQG YSEAIVDDIA ESKEDKNELA QIIHEESLRI GRLVNELLDL
ARMEAGHIQL YVESVDIHPY MNKIIRKFQG IADERDVKLT MRVDHEFDRL PFDSDRIEQV
LTNLIDNAIR HTQPGGKVEV TVDHINGDWI ASVHDSGQGI AEEDLPFVFE RFYKADKSRK
RESSKQKKGT GLGLAIAKNI VEAHHGTISV HSKLGEGTTF TFRIPKNLEL TEY
//