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Database: UniProt
Entry: A0A0F3KX39_9GAMM
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Original site: A0A0F3KX39_9GAMM 
ID   A0A0F3KX39_9GAMM        Unreviewed;       868 AA.
AC   A0A0F3KX39;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VI08_07625 {ECO:0000313|EMBL:KJV35835.1};
OS   Luteibacter yeojuensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=345309 {ECO:0000313|EMBL:KJV35835.1, ECO:0000313|Proteomes:UP000033651};
RN   [1] {ECO:0000313|EMBL:KJV35835.1, ECO:0000313|Proteomes:UP000033651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SU11 {ECO:0000313|EMBL:KJV35835.1,
RC   ECO:0000313|Proteomes:UP000033651};
RA   Sulaiman J., Priya K., Chan K.-G.;
RT   "Draft genome sequence of Luteibacter yeojuensis strain SU11.";
RL   Submitted (MAR-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:KJV35835.1}.
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DR   EMBL; JZRB01000014; KJV35835.1; -; Genomic_DNA.
DR   RefSeq; WP_045828932.1; NZ_JZRB01000014.1.
DR   AlphaFoldDB; A0A0F3KX39; -.
DR   PATRIC; fig|345309.4.peg.731; -.
DR   OrthoDB; 9770473at2; -.
DR   Proteomes; UP000033651; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          119..172
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          244..296
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          508..727
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          754..864
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         803
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   868 AA;  94706 MW;  3B2FDF36AEF2C30C CRC64;
     MTDSTQPNLN ADLSWLDGGG EVGALIRAFD WGPTGLGPLE AWPQSLRTAT GMLLLSPVPI
     VLLWGEKGIM IYNDAYSVFA GGRHPQLLGS EVRKGWDEIA DFNDNVMRVG LAGGTLAYRD
     QRLTLQRSGK PEPVWMNLDY SPVLDETGKP GGVIAIVVET TERVRAEERL RESESRFRAL
     VNSTSDIVYR MNPQWSRMIQ LDGRGFIADT TEPSPDWLAG YVPPDEQPRV REAIDDAVTS
     KGMFELEHRV KRIDGSIGWV ISRAVPVLNE DGDITEWFGA AGDISVRKAA EQALRENEAR
     LRFLDALNEQ TAKSTDADEI LSTSTRMVGE HLGVGICAYA DMDDDEDGFT IRGDWRLPGY
     SSIVGRYSLK AFGHLAVSRL RDGKPLIIED NRRELPPDES ATFQAIGVTA TICIPLIKRG
     KLTALMAIHD GQPRQWHLRE LALLDEVTER SWAHIARVRA EADVREGERR FREELEQQVA
     ERSAALERTQ AHIRQAQKME ALGSLTGGIA HDFNNLLMAV QGSLELLRER MPQDPLLLRL
     VDNARAGAER GSSLTRRMLA FARRQDLKYE RVDLRALVDG MTELMQRSLG PTVTVETHFA
     SGLPAVEADG NQLEAALLNL AVNARDAMDG VGTIVIGTSE AWVGAGDERL APGHYVRLSL
     ADTGAGMDEH TLKRATEPFF TTKGVGKGTG LGLSMAHGLA EQLGGALVLH SEPNRGTTAE
     IWLPAMAPTA EAPAAVRVEA PTPPLRGGTE GRFTIMTVDD DDLVRATTQE MLEDLGYVVL
     SARSGAEALR LLAASHVDLV VTDHAMPQMT GAQLAMQLRE QWPALPVIMA TGYADLPAGV
     QLDLPRLAKP YSQATLADAV ARALPAIG
//
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