ID A0A1T5FFN7_9BACI Unreviewed; 913 AA.
AC A0A1T5FFN7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN06295926_113127 {ECO:0000313|EMBL:SKB94947.1};
OS Lysinibacillus sp. AC-3.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1680467 {ECO:0000313|EMBL:SKB94947.1, ECO:0000313|Proteomes:UP000190941};
RN [1] {ECO:0000313|EMBL:SKB94947.1, ECO:0000313|Proteomes:UP000190941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC-3 {ECO:0000313|EMBL:SKB94947.1,
RC ECO:0000313|Proteomes:UP000190941};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FUYW01000013; SKB94947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5FFN7; -.
DR STRING; 1680467.SAMN06295926_113127; -.
DR Proteomes; UP000190941; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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 InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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:SKB94947.1};
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}; 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 511..743
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 791..908
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 428..501
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 841
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 913 AA; 103173 MW; E5359646662A8CF3 CRC64;
MLNKLKISIR TKITLGYIVI ILCLLASVVI LNNQITSLQK ERNYIIKNDS NIQALTNRIE
KYILDMESSQ KGFMITGELS YLEPYNRAGE SWELTFGELY QLLENKPAQQ QRLNEINATI
QHWITTVGEP SIKLKKEKNK EALWELYKVD IGSKDIETVR DQFESLRSEV IATMQAKVNE
LDKKNSVVTL TLLGILIFIS VVAIIIASSI SRSIVKTLTE VTRTIQEITA SKSNQKGRIH
VKTNDEINAL AAATNELLDA LERREWLQLN IAEIVTKYQG ISAITKLTET FLSEIAQKTQ
SSLGALYVRE TTDHQIQFEK KAAFADVTDN VGMESFKLGQ GLIGQCALEK KVLIYNDIPE
DFRLIGTGLG KIQPKGIFIV PIIFENDVIA IVELATLTSF NELQQELVKQ VIETFGLTIN
SVLGRMEIVR LLNESRALTE ELQVQSEELQ KQSEELQLQT EELTMINEQL EERTKEAELK
SRQLEQAKKE LEESAEQLLL NSNYKSEFLA NMSHELRTPL NSILILSEML AENSQNTLSE
EEAEFAKVIH SSGGDLLALI NDILDLSKVE AGKLDINFDE MNMSEVPVQI EQTFAPVAMK
KNLQFYISKD ENVVDIFYTD EQRFQQILKN LLSNAFKFTK QGSVHLDIKQ LREEQLTNNM
QDVSADWLEI RVSDTGIGIP KDKHQLIFES FQQADGATIR KYGGTGLGLS ICKELARLLG
GWISLQSNEG QGSTFTLTIP SLPNGIEEQE YLELAIHEVG ATNELEELME EQLLEAHDFS
QQEVEVFQGK NILIVDDDYR NIYALKNALE KRGMNILVAK DGIECLDIMQ ANDEIDLILM
DIMMPNLDGY ETMSIIRKQM KIMDLPIIAL TAKAMKNDRD KTLEAGASDY ISKPLNLDQL
VSVLRVWLVS KGS
//
