ID A0A286DCQ0_9GAMM Unreviewed; 1179 AA.
AC A0A286DCQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN06296416_109109 {ECO:0000313|EMBL:SOD56389.1};
OS Pseudoxanthomonas wuyuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1073196 {ECO:0000313|EMBL:SOD56389.1, ECO:0000313|Proteomes:UP000219374};
RN [1] {ECO:0000313|EMBL:SOD56389.1, ECO:0000313|Proteomes:UP000219374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10978 {ECO:0000313|EMBL:SOD56389.1,
RC ECO:0000313|Proteomes:UP000219374};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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};
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DR EMBL; OCND01000009; SOD56389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286DCQ0; -.
DR OrthoDB; 176203at2; -.
DR Proteomes; UP000219374; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07494; Reg_prop; 3.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000219374};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1179
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012470812"
FT TRANSMEM 767..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 821..1039
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1059..1173
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1108
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1179 AA; 127525 MW; 479B1A7B30335F65 CRC64;
MRWMLLLLLA LVPLPPARAG LPETPQLRQL TVADGLPSNI VYQIAQDQNG YLWLATADGL
VRYDGAGFRI WRQGEGLREN VVSSVAVDAD NRVWVGTLGA GVALLDRERE QFRYFDARSV
AGIGGDHIWS LLPTDDGALW FGTHDAGLHR MDRDGRVTRF MPQPDDPRSL PGAGVTDLQI
APDGSLWVAT DHGVARWTGH DFERLPDAAH PEMYVTSIRF DRAGNLWIAT VMGAGIYRPD
GSWSLDPWGL RQQVPVYGLL MEDSSGIHWL DTYDGMRRGE EGETFEVPLY SNLTRGRVKP
QWANALQDSE GGLWFASIDS GLWYLPPTWR QFSVLNKVEG VATSLGNTQV FDVAPSTSGD
MWLVGSSGAL DRLDPETGLV RRILEDVGNG TVAYAVAEAF DGQVWVGYPG GLLRYDPASG
AVRRWGADAG SDATAPADID AIAQAADGSL WIGQGARGVQ VRSPEGRVIR NIGFDGQHGL
AAGRAYSQLD LGPDGRIWLA CDGGVLAWDA GTGRFQPVPG LPQSQVDAFA TDGEGLLWLA
LPGALEGYRQ QAGQYRRVQR LGAEAGLPQV MLTGLTVDRR GILWAASNRG LARIDPVQPT
VRVYGIHDGL PGQEILSDPV KRLQDGRLVV SASHGLVIFD PLSLRPATTA PPLVVDAITV
RRASGPLALP LGQPFQLQHF QLEHGDRDLQ VTARLISYSN VQGHRYRFRL SDFDSDWVEV
GASGERTFSQ LPPGHYRLEV AGKTADNVWS QVQTIAFTVA PPWWRTWWAS LAAAAVAIAL
LGGLALAYRR RLRRRSAWQL AVHKHELAQQ ASEAKTRFLA TLGHEVRTPM TGVLGMSELL
LATPLDDTQR GYTQSIQRAG THLLRLVNDA LDLARIEAGK MELQSVAFDL HGLLDDVIAL
MAPVAEKRGL AFSARLAPTL PPMVRGDPLR LRQILLNLLG NAIKFTEQGQ VSLCADPLAD
QRVRLEISDT GPGINAEQQA RLFQRFEQAE GARTAARYGG SGLGLAICQE LAAAMGGWIG
VESTPGVGTR FVVELPLPAT AAPLPRKAQA PPLPARALMV LLVEDDATVA QVIAGLLRAR
GHRVSHAAHG LAALTEATTQ QFDIALLDLD LPGIDGLMLA RQLRQGGFAA PLLAITARAD
AEAEPQARAA GFDGFLRKPV TGDMLAEAIA QLMAHTETP
//
