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Database: UniProt
Entry: A0A098EYT0_9BACI
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ID   A0A098EYT0_9BACI        Unreviewed;       452 AA.
AC   A0A098EYT0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=ykoH {ECO:0000313|EMBL:CEG26557.1};
GN   ORFNames=BN1002_01405 {ECO:0000313|EMBL:CEG26557.1};
OS   Bacillus sp. B-jedd.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26557.1, ECO:0000313|Proteomes:UP000042335};
RN   [1] {ECO:0000313|EMBL:CEG26557.1, ECO:0000313|Proteomes:UP000042335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-jedd {ECO:0000313|EMBL:CEG26557.1,
RC   ECO:0000313|Proteomes:UP000042335};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) 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; CCXR01000001; CEG26557.1; -; Genomic_DNA.
DR   RefSeq; WP_048824242.1; NZ_CCXR01000001.1.
DR   AlphaFoldDB; A0A098EYT0; -.
DR   STRING; 1476857.BN1002_01405; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000042335; Unassembled WGS sequence.
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; cd00082; HisKA; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 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   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; 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:CEG26557.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000042335};
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        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          239..451
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   452 AA;  50195 MW;  12EA0C1D09C1A7D0 CRC64;
     MKLRLKINLY TAALFALVLI IMNLFIYLSF SKLIFTSHME SAEAEMKKSS AVVTQSLGKI
     PEAELLRAYV PVDGMIQLVG IDGKPVATVT SLSEKELAKR APNYLAGETG GRISYKGKDY
     SFQSMPVILP DGQVANLQMT TSLEPAVRIV GTLRLVLLLA TLAAMIPVLA SSAFLGKIII
     GPVTTMIRTM SDIRRSGQFK RLPLEGKSKD ELYQMGDTFN HMIDLLEANF DKQQQFISNA
     SHELKTPITI IGSYSSLLKR RGLQDPKLFE ESVEAIHSEA DRMKEMTEQL LLLAKHNEQW
     NLRMESVELG SLIFSAAKAF ENAFNREIVL DHSGKELILN TDEQKLKQLL FIFLDNAKKY
     SDAPISISFG SKGNEAFIEI ADKGIGIEED ELPKVFDRFY RVDKARSRKM GGSGLGLSLA
     KELADALGIR VELSSKPGIG TTAFLYLRRC DK
//
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