ID A0A0Q7U0J0_9MICO Unreviewed; 564 AA.
AC A0A0Q7U0J0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASD19_13045 {ECO:0000313|EMBL:KQZ06068.1};
OS Microbacterium sp. Root53.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQZ06068.1, ECO:0000313|Proteomes:UP000051407};
RN [1] {ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ06068.1, ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|EMBL:KQZ06068.1,
RC ECO:0000313|Proteomes:UP000051407};
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 -!- 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:KQZ06068.1}.
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DR EMBL; LMFR01000010; KQZ06068.1; -; Genomic_DNA.
DR RefSeq; WP_055989109.1; NZ_LMFR01000010.1.
DR AlphaFoldDB; A0A0Q7U0J0; -.
DR STRING; 1736553.ASD19_13045; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000051407; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQZ06068.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051407};
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 149..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..226
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 241..539
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 344..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 60186 MW; 4039C227B781A2F1 CRC64;
MAAGVGTVPI LRNAMLSNVD SSLTQLAAGA VGEQLFNISS SGDAGPTFTA KAGAPRTEYY
VAIYGPDGDL MASAGGQDPR QSRPDFPAKF GTDYAYSHQG SIILLDNTTG EGPGYHAAFA
VVQFPGSNNI YTQLVALPLD EVEKVVGTYF GIFFLVALVT IIGGALLTRW AVTLTFRRFG
QVEATAMSIA AGDFSQRLTD IEPSTEIGRL KAAINTMLDR IDDAIAERDA TVRQMRRFVG
DASHELRTPL VSVRGYAELY RMGAIQGDED TARAMERIEK EAIRMGVLVE DLLALARLDE
KRELDIQPLD LRPLARDAAL DVRAAEPSRT VTVIDTTIEA LTGPITISRP DEELPAEAGG
GADEAPRRRA RPVAANALTA LLRRRPRAAG EPAADTGEAE TAVPRLDFSV PQALRPVAVP
PIVLGEEHRV RQVIANLLGN ARRFSPEGSP IEIEVGVDVG AGMGWIAVVD HGEGVPEAIR
EQIFERFWRA DTSRARETGG SGLGLAIVAS IVEALHGSVE VRDTPGGGAT FRVAFPLAPR
TDEELALAAT RPMPRIRGAE TPSG
//
