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
//