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Database: UniProt
Entry: A0A1W5ZV98_9BACI
LinkDB: A0A1W5ZV98_9BACI
Original site: A0A1W5ZV98_9BACI 
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
//
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