ID A0A0A2WKP8_9GAMM Unreviewed; 873 AA.
AC A0A0A2WKP8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-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=LF41_930 {ECO:0000313|EMBL:KGQ20393.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ20393.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ20393.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ20393.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-2014) 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:KGQ20393.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRKJ01000002; KGQ20393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2WKP8; -.
DR STRING; 1300345.LF41_930; -.
DR PATRIC; fig|1300345.3.peg.251; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000030518; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 4.
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; 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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KGQ20393.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Transferase {ECO:0000313|EMBL:KGQ20393.1}.
FT DOMAIN 195..250
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 332..386
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 387..457
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 460..512
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 530..747
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 768..873
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 503..530
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 817
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 873 AA; 96862 MW; 9572F9BFEE026CE4 CRC64;
MLRSKFPMFV AWGPSMGFLY NDPYVEVLGA KHPFALGLPF EEIWSEIWED VGPLARRALA
GEATYMENLP LLMRRKGYDE PTWFTFSYSP VTDEQGDIAG MYCACTETTA GVIAERTRIA
QMQRLISLFE QAPGFVAVTL GREHIYEIAN PAYLEFVGRQ HIVGLSVRAA LPELDQKFID
ILTQVYDTGV PYIGNRIPVG LVRGNDGEMT DRIVDFVFQP IVDDHGRVDG IFIQGTDITN
QATAERLVET ERLRLEAVID SLPSGVALAN NEGDIIRVNA ANREIWGMHP TSGDVAAYGE
RQGWWAEDST RRGQQVAPDD WALSRALRGE VVRGDIVEIQ PFDDHPRRTL LLQATPVRLA
DGELAGAVVA QTDISDRVRA EADLRASEAR FRSITDAMPQ MVWSALPDGF NDYYNRQWYE
FTGLIPGEGE GQRWAEVVHP DDRVRAWARW GRSLDSGEDY EIQMRLHHHS GDFRWVLVRA
VPVRGDDGGI LRWLGTATDI HEHRIAQDAL ERSERALRDA DQRKDEFLAM LAHELRNPLA
PISTASQLLK LSSDPVRIRA AGDVIGRQVR HMTELVDDLL DVSRVTRGLV HLDLETVDFK
AIVISAIEQV RPLIDARGHA LRTRLPARAL WVHGDRTRLT QILANLLNNA AKYTPEGGEI
HLDAESDDGH VRVRIRDNGQ GIEPALLPRI FDLFTQADRS PDRTQGGLGI GLALVRSLVA
LHGGTITADS HGRDQGAVFT ICLPRVEAPP VAEDTHAHRI DGAGATLDVV VVDDNVDAAQ
TLQVLLEALG HRARVFHRAG DALNAIIESP PQVAFLDIGL PDITGHELAR EIRQRLGARA
GVLAALSGYG QPQDHAASRE AGLDFHLVKP WRC
//
