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Database: UniProt
Entry: A0A0M8PS12_9BACI
LinkDB: A0A0M8PS12_9BACI
Original site: A0A0M8PS12_9BACI 
ID   A0A0M8PS12_9BACI        Unreviewed;       379 AA.
AC   A0A0M8PS12;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AN161_14395 {ECO:0000313|EMBL:KOS62114.1};
OS   Lysinibacillus sp. FJAT-14222.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1932366 {ECO:0000313|EMBL:KOS62114.1, ECO:0000313|Proteomes:UP000037693};
RN   [1] {ECO:0000313|EMBL:KOS62114.1, ECO:0000313|Proteomes:UP000037693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17725 {ECO:0000313|EMBL:KOS62114.1,
RC   ECO:0000313|Proteomes:UP000037693};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOS62114.1}.
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DR   EMBL; LIYL01000031; KOS62114.1; -; Genomic_DNA.
DR   RefSeq; WP_053595045.1; NZ_LIYL01000031.1.
DR   AlphaFoldDB; A0A0M8PS12; -.
DR   STRING; 1932366.AN161_14395; -.
DR   PATRIC; fig|380630.3.peg.3250; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000037693; 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; cd00075; HATPase; 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; SSF158472; HAMP domain-like; 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:KOS62114.1};
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        89..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          108..161
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          169..379
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   379 AA;  42343 MW;  D7DDB09A0CE8DA31 CRC64;
     MFKKMPIRLR LTVMMVILLT ICCVGLTLIL NFSAGIMATR IDAAVLSPAQ VVGEDSNIID
     NLQTPSNAMM TTPSEDVQEA RTDFQIKSVF YLLLVIVGGG ILTYYVSGKV LKPLDTLNSQ
     IKNRTVHNLS ETMDIPPTND EIAELTQSFN EMTDKLNDAF MMQSRFSASA AHELRTPLAV
     LKAKVDVFKK KHTHSTEEYI ALISVFEKQT QRLSELVRSL LDMTNMNVGF ENETICLKDV
     LEDIVSELSH IANEKNVTLY LDCADAVVYG NIDLLYQAFY NLVENGIKYN IDGGKVMIKV
     KSDKKQIIVD IKDTGIGIPD EEKKNIFEPF YRVDKSRSRE MGGSGLGLSI VQSIINKHNG
     KITVTDNKNG GTWFKIILN
//
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