ID D0R4C8_LACJF Unreviewed; 499 AA.
AC D0R4C8;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=FI9785_1075 {ECO:0000313|EMBL:CAX66941.1};
OS Lactobacillus johnsonii (strain FI9785).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=633699 {ECO:0000313|EMBL:CAX66941.1, ECO:0000313|Proteomes:UP000002627};
RN [1] {ECO:0000313|EMBL:CAX66941.1, ECO:0000313|Proteomes:UP000002627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FI9785 {ECO:0000313|EMBL:CAX66941.1,
RC ECO:0000313|Proteomes:UP000002627};
RX PubMed=19767436; DOI=10.1128/JB.01182-09;
RA Wegmann U., Overweg K., Horn N., Goesmann A., Narbad A., Gasson M.J.,
RA Shearman C.;
RT "Complete genome sequence of Lactobacillus johnsonii FI9785, a competitive
RT exclusion agent against pathogens in poultry.";
RL J. Bacteriol. 191:7142-7143(2009).
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; FN298497; CAX66941.1; -; Genomic_DNA.
DR AlphaFoldDB; D0R4C8; -.
DR KEGG; ljf:FI9785_1075; -.
DR HOGENOM; CLU_000445_89_6_9; -.
DR Proteomes; UP000002627; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR025711; PepSY.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF03413; PepSY; 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; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAX66941.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002627};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAX66941.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 141..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 234..406
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 475..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 57529 MW; 0779FA74ED33B551 CRC64;
MILSVKLTQL FLTLFIIILF LVNLAFAGIS TAFIYNNAHE QAEEVIDTVS DNISDHDEHK
NKNEWKLFLN AYLARQSNDA ISLKTPKGKT VYSEDGEELF EKVKNHKNYN NVVFMENSVY
YLRTAAEDGY QISVILNVDD LFTLITHLLL AIIILNLIAI ICSIPLIKRF SRKWSQPIEK
IDQDIEAIEH QTTAKKKVFV PKQPAEIHHL AQSFNKLLEY QDKAIQREQQ FVTDASHELK
TPLAAIRGNI NLIKRLGKEH PEIIAKSLQY IDSESSRMEI LFNELLELGR AKKQHQSIGP
IDLVPIVQKE SEILEQEYNT CSVYISSPTK IFYPIEVKDF RLIIHNLLDN AAKYSQNNAK
INIELQKDHV YLTLRVKDQG IGIREENYDK IFDRFYREDQ AQAFTGGQAT EQTQTSNSIS
LSQSDAINKF NEKYGSKSIK GIELKNKKNE YIYEVEGFDS EKEYKVKIDA KSQKILRTKT
DGDKKDKKRK EGSSRSQRK
//
