ID A0A0Q9TU07_9BACL Unreviewed; 605 AA.
AC A0A0Q9TU07;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG93_20325 {ECO:0000313|EMBL:KRF42907.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF42907.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF42907.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF42907.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF42907.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF42907.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRF42907.1}.
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DR EMBL; LMSP01000002; KRF42907.1; -; Genomic_DNA.
DR RefSeq; WP_056829732.1; NZ_LMSP01000002.1.
DR AlphaFoldDB; A0A0Q9TU07; -.
DR STRING; 1736411.ASG93_20325; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000051948; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 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};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..376
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 483..586
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 364..396
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 605 AA; 69072 MW; DA8D0A03C3F1F37F CRC64;
MRLNVKRWKV SSILYIMFVL MIVLPISMVA FFSLRAYTQI LLENSTSQTI QTLKQVSYSL
SQENSRYIHT IASIATDKSV LELTASLHHE KDTQSHFKYT VQLDEQMKGY FHDMPDLISA
TFIFRDGSSY YYEGPQYYEH LTSDVESLRQ LRGYKQALSA EGHVQMLGTQ VKFSGNLDSK
YILSAAIAPR SNPLLHDVEM IYFFYKSKAL ENLADSSKND SGFVVLDSDG EVMLATGGTN
QTKGLEPRAI EKAMLDQSGH YNTIVQGMKM FITFLTMDST GWKLVYLIPY NQLTYQFKQI
YYTMMEISGA GFIFFLIVSV FMVRRLSRSI SMLVRQMNRV KSGEFDVKIT ATGPLEIHLL
GKTFESMVLR IQELMRELRE REKQKTHAEI DALQSQINPH FLVNTLSAIK VMAMISKNTN
IYEMTDSLVK ILSSTFNRNG SYIQLKEELM YLEKYIHIMK IRYGDRFKVE FSFQEGILET
YVLKLLLQPF LENAIHHGVQ ESEPFGYIHI TGKKENECLV LLVQDNGRGM DQQTAQSLLR
KHAINGIGIA NVNDRIRLNY GEAYGVQIQS EVGSGTTVTV RLPLILTIPE ELNNLGTISS
TKGNQ
//
