ID A0A3D9JM82_9BACL Unreviewed; 605 AA.
AC A0A3D9JM82;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DFP98_117120 {ECO:0000313|EMBL:RED75148.1};
OS Cohnella phaseoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=456490 {ECO:0000313|EMBL:RED75148.1, ECO:0000313|Proteomes:UP000256977};
RN [1] {ECO:0000313|EMBL:RED75148.1, ECO:0000313|Proteomes:UP000256977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7287 {ECO:0000313|EMBL:RED75148.1,
RC ECO:0000313|Proteomes:UP000256977};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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:RED75148.1}.
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DR EMBL; QRDZ01000017; RED75148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9JM82; -.
DR OrthoDB; 9762826at2; -.
DR Proteomes; UP000256977; 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; 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; PTHR45453:SF3; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 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:RED75148.1};
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 9..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..370
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 392..590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 605 AA; 69901 MW; 9E73F78427B8500D CRC64;
MNKGIVLKLF LFTMALCMFI LAVIFTLQTV FFKQFYVHQK VKNVNTALQA YKQDYLNQAS
STQEMAKLEQ IFFQKHNTWI TVLDTRGNLK YADDFFMEIK LDRSEESALF DKTITVPLYS
FINVEDFSSN KTFLTPWIQE GERIALEGLI TNNQPVIQRM GRSTSNLRDE SRLENHQIAS
KEYEVVDRSN IIQYREKYSP FLVKGTITKV RIPEGAGVSR YTNHLFLDRI KAFQADLLYG
DFKDATNASQ IVDYEENHAN YKIFVDRIQD RDGNPTYLFA MTSLQPVNEA AGMIQDYYVY
IIIATLLLVL LASFYYSRQI ARPLLRINRT ARQMADLDFS EKIPITTKDE IGDLSRSINE
LSERLHSHIL RLQQDIDKEK QLEYTRKEFI SGVSHELKTP LSVIQSCLSI LKDGVVSHKR
DHYFAAMEDE VRRMDLLIAD MLELAKYESG TYKMDVGSFY INIVIERVCT KLTPDIQAKR
LLLNTSLKSV EVEGNERRIE QVIVNFLTNA IRYTPDRESI LVTTSEERDI VQICIENKGA
HIPDEQLEKI WERFYRGEPS RHRSTGGTGL GLAISKKILE MHGVAYGVIN TSDGVLFYFH
LNKKG
//