ID A0A0A2WJ29_9GAMM Unreviewed; 2067 AA.
AC A0A0A2WJ29;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LF41_461 {ECO:0000313|EMBL:KGQ18707.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ18707.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ18707.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ18707.1,
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 -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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:KGQ18707.1}.
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DR EMBL; JRKJ01000017; KGQ18707.1; -; Genomic_DNA.
DR RefSeq; WP_036169622.1; NZ_JRKJ01000017.1.
DR STRING; 1300345.LF41_461; -.
DR PATRIC; fig|1300345.3.peg.2134; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000030518; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 5.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 642..749
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 812..917
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1295..1399
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1538..1790
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1792..1924
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1942..2058
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1179..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1562..1589
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 689
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 857
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1342
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1991
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2067 AA; 224502 MW; F5BD4C1F4BD38681 CRC64;
MTALRDAIDT TTLGWIKPEI DETLRQARRD IEAFAEDPSD TNYMRFCASF LHQVHGTLRM
VELYAPAMVA EEMERLALAL VVPQGAVGAV ADRDEACAAL MRGVVLLPDY LERLQGGHKD
IPIVLLPLLN ELRAARGETG LSESVLFAPN LDRPLPEDLP APMALPRQSR QLMAGQQLSS
LRDALAQWPE DGAPTNIGGI AKAIDGLLES ADHEATRRML WVASSVATAL RDGALPATKA
LRQAFAGVER EARHVFEGDG FNARGEPTAE PTRQLLYHVA HNEQSHNALD ALRSTFDLAA
QMPTESELAH ARGSLSGRNR ALLDTVAAAI KEDLLRVKDS LDLHLRTKQT GVSDLQPQVE
ALSRVADTLG MMGLGVARNV VLQQRDAMHD IVAGNRPADE GALLDIAGAL LYVDASLDDQ
VARLGRADSE DGDTIGAESR KVLDILIREA IANFADARQA FVAFVETSWD HSQLTDVPRL
LDEVGGALRI LELPQPAEYL TGIGRYTNNE LLARKRVPNG QQLDTLADAL ASIEYYLEAL
RDNRPSRDGI LDIARQSLET LRYWPLPAEE KADAEAPADI AIETPAAEVE APTAFVSTPT
EPVAAAPITF VSEATQPVVE APAAATAAPV ATGVAGGFEA TSDDIDDEIR EVFLEEFEEE
IGHLETMLPA WRAAPEDNEK LRPIRRVFHT LKGSGRLVGA KTLGEFSWKI ENMLNRVLDG
TRPASPAVIG LVEQAFYTLP QLHAALRGEA PLTADLAGIE AIADRVAAGE EATYVASAAP
VVSEATAPVV EALVEDTIEV ATPVVEDEPT IAAKVDPVLL EILGTEVGGH LVTIDAWLAQ
AQSRPIAAND ALLRAMHTMN GAFAMTEVPA ITNLTGPAET YIKRMLAAHA VPTVQGVAAL
AATAEAIRRT VEALQSDAPR VPVFESLARQ VAELRDSLPE AKMPLLPTEP VELEAAELTG
GVDLSEFTDL AGDAPVDTGL QLQDEPLDTP VADDIIVSED LSAFLDLATQ IPVDNGMPAN
APEAEALAES DFEEIVLEEI VLDGEVEAPA FDAIAFDDAS IESVTLESPQ VETIELESGE
AFDAAAIDAQ AALEASLLDA ERVEAERLEA EQRLQALETA ERLEAERIEF ERVEAEAAEA
ERLAAELAEI ERLEAERLEA ERLEAERVEA ERLEAERLEA ERAEADRAEA ERVEAERAEA
ERAEAERAEA ERAEAERVAA EEAEEYARLE AEYEAQRLEA ARAEAEAAQS IAPVEEPVAE
AEPEVEAEPE SEPAVAQMLA DAMAGHGDPD EALDITDLDP ELVDIFCEEG GDLLDHSDGL
LAHLRENPSE REHLVGLQRD LHTLKGGARM AGIMAVGELG HAMESLLEAV VEHRSELGRD
GIPLLERGFD RLHAMVTRVS ERRAIAMPEA LIAEFDARAK GRTYEPAAEV YERPVHIQPK
AELKPLSAPM DSQPTGEDDD TSVRAPQEQV RIRADLLDRL VNYAGEVAIY RSRLEQQLGA
FRGAMGEMEQ TNARLRDQLR RLDIETEAQI IARYQREDTA DATFDPLELD RFSNLQQLSR
GLAESAADLT SLQGSLEDLT RQYETLLLQQ SRVSSELQEG LMRTRMVPFD ALVPRLRRVV
RQAAGETGKN VQLKLEGAQG ELDRNVLERM TAPLEHMLRN AVAHGLEAPS ERKKHKKNEE
GTIRIAVRRE GSEVVLEVGD DGAGLNRNAI RKRAEERGLI RSDAVLADAD LDALIMEPGF
STADTVSRLA GRGVGMDVVA SEVRQLGGAL DIKSREGQGT TFTLRLPQTL AVTQAVFVKI
GETTYAVPIA SVRGVGRISR DQITGEESYT YGGEAYGLHD LGLLLGHAAA KAEGQLQMPL
LLIRSGELRA AVSIDQVVGN REIVVKPVGP QVGSVPGIFG ATIMGDGSVV VILDVAPLVR
RQASMPRDVA PQPQPEARRV PLVMVVDDSV TMRKVTGRVL ERHNFEVATA KDGVDALEKL
DERVPDLMLL DIEMPRMDGY ELATAMKADA RLRNVPIIMI TSRTGEKHRQ RAFDIGVERY
LGKPYQEHEL LRNVFELLAE QGGPRNG
//
