ID R7Z9M5_LYSSH Unreviewed; 505 AA.
AC R7Z9M5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=H131_19332 {ECO:0000313|EMBL:EON70860.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON70860.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON70860.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON70860.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) 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:EON70860.1}.
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DR EMBL; AQPX01000027; EON70860.1; -; Genomic_DNA.
DR RefSeq; WP_010860773.1; NZ_KB933402.1.
DR AlphaFoldDB; R7Z9M5; -.
DR PATRIC; fig|1285586.5.peg.4029; -.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OrthoDB; 9792991at2; -.
DR Proteomes; UP000013911; 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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF14; SENSOR HISTIDINE KINASE CSSS; 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:EON70860.1};
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|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..272
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 287..504
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 505 AA; 57829 MW; D35C91A7AC9120CB CRC64;
MRKISKLFLY LLNKLKKLIV NAITKVRQSI RIQLLTTFIL CAFLGLLAAR ATLPFVLNIY
QTATIDYSQG MQQINFQAQR AADIAINENS VVSLQQMIEA ENVKLEMKQS ALNVIVTDES
GKVIYKTKQV EEEHINLHNK IRHVMDFAIN HPLYNYEIPA IEQLQQEFIA FYPLTIEDKN
LYLFVSGIPE GVVIASSTEG LIPLFIAIAV FTFSFFYITK RKMNQIEALA KGVMEMAKGN
LAYRIEKKGI DEIALLTENV NHMAEAIMTT IAKERRIEKQ KNELITNVSH DLRTPLTSIM
GYLRLLREGR YDTREQYEDY IKIAFSKSEQ LKNLIDDLFE YTKLTNENIV LNQHNVCINE
LLDQLIEELV PQAEERNLLF EKNYPEERIY ASVDSEKIVR VFDNLLMNAI KYSTSGGEIK
VSFKKQQNSL QICVANHSEQ FTKEELVNLF ERFYKKDQSR TNVSEGSGLG LAIAKSIVEL
HGGEIGANYE DGLLQFTILL PISAQ
//
