ID F2F131_SOLSS Unreviewed; 938 AA.
AC F2F131;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SSIL_2403 {ECO:0000313|EMBL:BAK16826.1};
OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK16826.1, ECO:0000313|Proteomes:UP000006691};
RN [1] {ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA Morohoshi T., Someya N., Ikeda T.;
RT "Genome sequence of Solibacillus silvestris StLB046.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAK16826.1, ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK16826.1,
RC ECO:0000313|Proteomes:UP000006691};
RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT "Complete genome sequence and characterization of the N-acylhomoserine
RT lactone-degrading gene of the potato leaf-associated Solibacillus
RT silvestris.";
RL J. Biosci. Bioeng. 113:20-25(2012).
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; AP012157; BAK16826.1; -; Genomic_DNA.
DR RefSeq; WP_014824075.1; NC_018065.1.
DR AlphaFoldDB; F2F131; -.
DR STRING; 1002809.SSIL_2403; -.
DR KEGG; siv:SSIL_2403; -.
DR PATRIC; fig|1002809.3.peg.2419; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_16_9; -.
DR Proteomes; UP000006691; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAK16826.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006691};
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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 586..800
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 820..935
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 261..292
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 869
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 938 AA; 108386 MW; 0E39824F12C52F32 CRC64;
MPRLIPTFKK NIRNQFVRML WSIIILFTII VGAFFIYTNV TNERLISERE AISEKEQLVQ
KMNESFNDIF FRARGYYAFK DKNELNILYD QMSVFEMELQ KFGEMPLSSE ENLLYEELNQ
FIVTYRNEIL PKAVSYVEAD NYEALRDLSN SGANESVNSF IAYTKSYTTE TDMVVNDHFN
RTLDQIKFLT VLCIFLFIIV FIIIGIILKR VIQNLISPIE KLTTATDAFA TGDYVDITPL
KNKEDELGVL ATSFYNMTRS IQEKEEVLTT QNEELMAQQD ELQGNQEQLQ QSLSHLQQYN
ELNHVLTFTL DKEKLIEDLH NYLRSIYEFD SSLMYLIDSG EFVSKGLAKE TTERLIKHLE
IDKIARLEEE KTFVICREVK SASNIANTTY NDYDLYTCIL NSEKKLVAIL MATREGRSFS
SKELTDINGH MNQASIAFER IFMYEEVERS RKLNQTIIDT TNEGIQFVSK YGEVLLLNKA
LFNIIRYPFE EIDDKVPQQL WLKHFQKIAE ESDELVYFLK IAIIEEFTNT RTMRYSIQQD
GRSPVFVEVY ATSVFEGDEK VGTMFVHRDI TSEYEVDMMK SELVSTVSHE LRTPLSSVLG
FTELLLAKEI KPERQKKYIE TIHKEAKRLT NLINDFLDIQ RIESGQQVYS MNKISLTALI
EDVLKNFQID PQHNIRFVDE STNAIVSADE ERIIQLLFNL IGNAIKFSPN GGEIIIRMQN
INETVQVSIQ DCGIGIPESA IPSLFQKFKR VDNSSRRKIG GTGLGLALSK EIISKHKGDI
WLESEEGIGT TIFFTLPLYD QEIVENRNEL TEEKTISNRT VMIVEDDLSL ALLLSEELKS
KGFTIIYHDD LKRAYDDAIQ IPLVGIVIDL IMGENMDGWD LVEALRNHKN TKEIPIIISS
ALDKSSVNMD KYNVEEYFTK PYPPEELSTL LLKFVKDQ
//
