ID A0A0G9H6M4_9GAMM Unreviewed; 2038 AA.
AC A0A0G9H6M4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Y882_03020 {ECO:0000313|EMBL:KLD65495.1};
OS Dyella japonica DSM 16301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1440762 {ECO:0000313|EMBL:KLD65495.1, ECO:0000313|Proteomes:UP000035481};
RN [1] {ECO:0000313|EMBL:KLD65495.1, ECO:0000313|Proteomes:UP000035481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16301 {ECO:0000313|EMBL:KLD65495.1,
RC ECO:0000313|Proteomes:UP000035481};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
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:KLD65495.1}.
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DR EMBL; JPLA01000006; KLD65495.1; -; Genomic_DNA.
DR RefSeq; WP_046970382.1; NZ_JPLA01000006.1.
DR STRING; 1440762.Y882_03020; -.
DR PATRIC; fig|1440762.4.peg.3381; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000035481; 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; 3.
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; 4.
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; 3.
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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 687..794
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 878..982
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1247..1351
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1514..1747
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1749..1886
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1912..2028
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 734
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 922
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1294
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1961
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2038 AA; 222546 MW; A77192F596AC0B9F CRC64;
MRLQDHIDFT TLQWVKPELD ETLAVAREAL ESYVDNPGNR DAMRSCADSL HQVHGTLRMV
ELYGAAMVTE EMETLAISLL EDHVANREEA YAALMRGLMQ LPDYLERLSG GHRDVPVVLL
PLLNDLRSSR GQQALHESAL FTPNLEFPLP AQAPTPPTEL LVERQRSEVT TLRLRFQQQL
LSWFRGQGND QQLGGMIQTL DAITARCHTI PGRRLWWIAA GVLEGVQQGA LKSQTGEVRQ
LIGKVDRSIR QLVEHGEANL RGGDADELAR KLLYVVGQVR QGSPRMELLR QTYSLDALLP
EASEIEHARG SMAGHNRALL DSVAKALKDD LLRVKEALDL FLRQTDADPA QLSSQTEVLE
RVGDTLGMLA LGVPRRVVNE QRRVLEEIAS RVRAPDEELL LDVAGALLYV EASLDDHIES
LGADGETTAE MPTAMLPRSE ARHILATLMH EATANTGKVK DAIVAYVESG WQSTQLADVG
ALMDEVAGAM RMLSAPRPAE LAEGIGRFVG NELLADRRVP STAQMDHLAD ALAALEYYLE
AAREHRGGLE HILDVAEHSL SSLGYWPPPA VRAPSEDELD EPPVEVARAA DAALAAALAN
QPELSESVSL GHGEDLSGLI VGHSDTPEPA PQEITGLRLA DTVHVTPQEP VQAAEDDWIE
IEEEILEEVP VSGSGYAAIE AGFQSSTAGI DDDIRDIFLE EMQEEIDNLH AARKTWLADP
QQIDSLTSIR RSFHTLKGSG RLVGATMLGE FAWKVENMLN RVLDQSIPPS EGVQEVVSAA
IDALPQLRTA LTGDGLVTAP LTAIMEISER LSAGQADARL ADIAPAGGTE TVRRVVRRRV
PRVDTSAEAI PASSLAQIES SPVEPVAPVH EFIATPVMPP IDPVLLEILR SEVAQYLATI
RTAINRTDGE LRVEDSLLRA VHTLHGAIAM VDIPVLTQLL SPLESLLKRL RAAGLPLSPE
GVMLLSQSAD AVDHVMGQFD VPSPQLPDLD NLIHRLTELR DSQPEPQVAH VLFETPADVS
DEAPLQAAEP THEASLGASL DEALSDASQP VEHIELAAPP VVSETDKYTD ELLAALGEFD
LDAHLPTAEQ SAHHAPTQVP VTDEDDFSKA YADLLDDAET LEIGPVVDEA EASVEHVATP
AAELDETAPS IEIESAEPEL EQLAEPVIEH LEPVEEITLE EITLEETPIE ETPIEEIVLE
APVLDAPELP SEEALVEAAA APEAEVEATP TQEAAPEEVI DENALLPSQI DPDLLEIFIE
EAREILDHSD GVLALWRAEP SAIEHLGEIL RDLHTLKGGA RIAGMVPVGD LTHAIETALE
RPIHAESAHI GELIAALEVG FDKLHGLVQL VSQGRPVAYP QAVIDRFLAM AGEGETAAHA
EAPEAPNVVP FPARPVVLSE PLPDLLPELL PEEREDAPST PQEQIRVRAE LLDTLVNHAG
EVAIYRSRLE QQVAGYRFNL VELDQTVQRL RSQLRMMEIE TEAQIIARFQ REHREAGISV
FDPLELDRFS QLQQYSRALA ESVSDLVSIQ GMLDELTRQA ETLLIQQSRV SSELQEGLLR
TRMLPFDTMV PNLRRTLRQA AQEEGKGAQL YVEGAHGEMD RNLLDRIKAP FEHMLRNAVA
HGIESPKDRR KAGKPEEGAV RIRVAREATE VVVRVTDDGR GLDRDAIRKR GIERGLIRND
TRLSDDQVLA LITQPGFSTA SSVTQLAGRG VGMDVVANEI KQLGGALSIE SKEGQGTTFV
LRLPFTLAVT QAILVRIGES NFAIPMTSVQ GVARISPAEL AERMAEPEPT FVYGGESFDI
HHLSELLGAV TTHVGDDEQI PLLLTRAGDL RAAIRIDAVI GSREIVVKSV GPQISSVPGI
LGATIMGDGS VLIILDLAPL VRHGIARRLQ RLDEGLTAVA TPVVEEQRVR PLVMVVDDSI
TMRKVTGRVL ERHEYEVATA KDGVDALEKL HERVPDLMLL DIEMPRMDGY ELATQMKSDP
RLRDVPIIMI TSRTGDKHRQ RAFDIGVDRY LGKPYQEAEL LAQIGEVLEQ RITESLNG
//
