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Database: UniProt
Entry: A0A0M2LYQ9_9MICO
LinkDB: A0A0M2LYQ9_9MICO
Original site: A0A0M2LYQ9_9MICO 
ID   A0A0M2LYQ9_9MICO        Unreviewed;       505 AA.
AC   A0A0M2LYQ9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=XM48_00760 {ECO:0000313|EMBL:KKI22640.1};
OS   Leucobacter sp. Ag1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI22640.1, ECO:0000313|Proteomes:UP000033836};
RN   [1] {ECO:0000313|EMBL:KKI22640.1, ECO:0000313|Proteomes:UP000033836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKI22640.1,
RC   ECO:0000313|Proteomes:UP000033836};
RA   Pei D., Kukutla P., Yu W., Xu J.;
RT   "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-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:KKI22640.1}.
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DR   EMBL; LAYO01000046; KKI22640.1; -; Genomic_DNA.
DR   RefSeq; WP_046453865.1; NZ_LAYO01000046.1.
DR   AlphaFoldDB; A0A0M2LYQ9; -.
DR   STRING; 1642040.XM48_00760; -.
DR   PATRIC; fig|1642040.3.peg.3429; -.
DR   OrthoDB; 9767435at2; -.
DR   Proteomes; UP000033836; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.450.280; GAF domain; 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; IPR038424; H_kinase_PdtaS_GAF_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR022066; PdtaS_GAF.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR   PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR   PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07568; HisKA_2; 1.
DR   Pfam; PF12282; PdtaS_GAF; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033836}.
FT   DOMAIN          299..490
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   505 AA;  54977 MW;  4553421B38229A2A CRC64;
     MSTLQNLAEK YSNLSQEEIE WLDLLVLDWP LLADLALGDV VLWAPTDAGE YLAVAHSRPA
     GSVTLFYRDV IGDFLRPDWR DLVDEAMTTR APVVSTSPAW YEENPMNLTA FSVSRRDEQG
     RLQGPFAVVT LHTSSADQQS ASRIGAAFRE CASDLFSMIQ HGLFPSPGTT KGRERGAPRA
     ADGLVRVATD GEVTFASPNT QTTFTLLGYR DELEGENLSE VLAELLKGQF DTNESLPLIT
     QGKIAKRADI EARGRVATLR SIPVIRDGER AGGIILTRDV TDLRQQEQEL ITKDATIREI
     HHRVKNNLQT VASLLRVQAR RARSEEAKEV LGQAMRRVAA IAVVHDTLST GLSQIVDFDV
     VFDRVLGLAA EVASLHGTTV HPSKEGKFGE LPSEYATPLA LALTEVVTNA VEHGLAGREG
     EVIIRADRTD DRLAVEVIDT GSGLPDGRVG DGLGTQIVRT LIEGELGGSI SWGSDARGGT
     RVAIEVPLHW IRTDTREIPR VSTTV
//
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