ID A0A031IMN4_9BACL Unreviewed; 679 AA.
AC A0A031IMN4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BW42_01401 {ECO:0000313|EMBL:EZP61730.1};
OS Exiguobacterium sp. RIT341.
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1470592 {ECO:0000313|EMBL:EZP61730.1, ECO:0000313|Proteomes:UP000023864};
RN [1] {ECO:0000313|EMBL:EZP61730.1, ECO:0000313|Proteomes:UP000023864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT341 {ECO:0000313|EMBL:EZP61730.1,
RC ECO:0000313|Proteomes:UP000023864};
RA Gan H.Y., Gan H.M., Savka M.A., Hudson A.O.;
RT "Draft Genome Sequences of 13 Willow Endophytes.";
RL Submitted (MAR-2014) 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:EZP61730.1}.
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DR EMBL; JFYW01000001; EZP61730.1; -; Genomic_DNA.
DR RefSeq; WP_035408821.1; NZ_JFYW01000001.1.
DR AlphaFoldDB; A0A031IMN4; -.
DR PATRIC; fig|1470592.3.peg.1382; -.
DR Proteomes; UP000023864; 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; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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 PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 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.
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:EZP61730.1};
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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..130
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 456..672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 122..156
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 679 AA; 77932 MW; 2B6C8D5FA317B973 CRC64;
MKHWMTEKLG RQLMAIFYSV FALSVITSVA SYLYVDNADG RTKEQVLDQL QKTQWFWFLN
LMVFLFCLLF IVRPLIHRVT SQLRELNVKS RRLAEGKSIS LEHDVDSHNE VGQLTASFYQ
MARSISSQHA ELSAKNQEMK RNQEVLTQKQ DELEHALEVT RTNELHLQDR NELIETLASK
ESLFDYSSVI STIVRLTKTE FGALLLIKNN EIAQVVPKEM TEDQQESLKT ESLLLKRVMI
SKETAHSSKK VANDDLIKYP YHVYEGVIPI MDPAKEELIA CLYLARFDAP FNQQDLAELE
SFSKQIAISL MRMSLYEQME YERKETAQLL NSVREAILYI KHEEKTILGN QALFDIFQSL
QVEEDNDSMT FLEVQPETMF EQMDQKEAFE AYFEEVLSGE IPEGMFSLSI DQGEYFIQVY
AEAIAHGEQS KGTILVFRDV TAETEVDRVK SELVSTVSHE LRTPLSSIYG FTELMLKRDL
DPERNKRYLQ TIHDESKRLT NLVSDFLNVQ RMESGKQEYD KQIFDLKEIV KEQIQFYQAA
TEQHSLQLDL NDEQDFMVEA DANSMKQLLG NLLNNAVKYS PDGGDVVVTL THQHNQIELS
VRDFGIGIPS HSMPHLFSKF YRVDNSDSRK IGGTGLGLSI CKEIVRAHDG NIEVESILGE
GTVFRVKLPS ATDALLEAE
//
