ID A0A1I2FV48_9BURK Unreviewed; 2002 AA.
AC A0A1I2FV48;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN04489711_11212 {ECO:0000313|EMBL:SFF08698.1};
OS Paracidovorax wautersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=1177982 {ECO:0000313|EMBL:SFF08698.1, ECO:0000313|Proteomes:UP000199119};
RN [1] {ECO:0000313|EMBL:SFF08698.1, ECO:0000313|Proteomes:UP000199119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27981 {ECO:0000313|EMBL:SFF08698.1,
RC ECO:0000313|Proteomes:UP000199119};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FONX01000012; SFF08698.1; -; Genomic_DNA.
DR STRING; 1177982.SAMN04489711_11212; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199119; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SFF08698.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SFF08698.1}.
FT DOMAIN 704..808
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1048..1150
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1223..1325
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1469..1702
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1704..1840
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1876..1992
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1417..1444
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 751
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1094
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1270
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1925
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2002 AA; 212715 MW; 4C79B7DE9EF831BC CRC64;
MPFMDAAHAS AAEGAPPPEQ DLGPLAWVHE ELRKSLDGAL KSLRRFVREA AVARESDLAA
LDSSALRMAR QQLHQASGAL EMVGMAAPAL VLRSMEAAVQ KFVQRPDQCG EEAVAVLERA
SFALVEYLEL VLAGKPASPV ALFPQYRDVQ ALTGAERVHP ADLWPVEREL REPEMPLPEA
PLPYGPAARA RLDSAVLRIV KHGDAAAAGQ MRDVCLGLAA ANAEREPRTF WKLCAGFFDA
FAAGLLPTDV YVKRVASRVL MQYASLAKGD AAIADRLVQD LLFFCAQARV PAGDAAGATP
LHAVRQTFGQ QAATPVDYEQ PRFGRHDPAV LAQARRRIAA TAETWSALAG GDRSKHKPAA
DQFGLVCDSL ARLYPGSEAL AGALTRAVET AGRAGGVPPP DLAMEVATSV LYLQAAFEEP
DTAQAHLAER GAELAQRLDH VAAGGEPAPL EAWMEELYRR VSDHQTMGSV VGELRASLAE
TEKAMDQFFR QPEDLSSLTP VPDRLAQMRG VLSVLGLDQA SLAALRMRDT VERLLAGQVA
EAERPALFEK LGNSLGALGF LIDMLGYQRS MARKLFVYDE VQGELRLRMG RARELAHRAR
QAQEQERAPE PAPQPAPAAE PAAVPPEALA EEIPAAVAAE PEPAPVPAQA AEPEQETPTP
AEPGFTLDLD ALDFPAEQGA AESLAAAVPL APEPLPPAQP LPDADDEDQE LLDIFLDEAR
EVVATGLAAV QSLRAAPGDL SEQTTLRRAF HTLKGSSRMV GLALFGDAAW AMEQALNAWL
AEQKPAPADL LDLSEQSLQA FGRWADAIAA GDDSGWQAQP FVDAASALRA GQTPEPLRVP
GAEGLPAAAP EPSSGDLPAS AEEHAADTEA EALAVDEEGG LPSAEAAPVD DAEALPAQEI
DFADFMQAVE ASDAAEAAQA PDPAGEPAAA DVEADADAAV AGTSEAEALP PASQEPEPLV
AHDTVPTLDL ADVVELAEEA ATEPESPVAA EACQADEALP PELPAPEDVP AAVESSEPLE
PPAAQESEEL AETLEPAPSD EAVKVIGTLR IGIPLYNVYL NEADEWSRRL STALQEWSLE
LHEPLPDMAV ALAHSLAGSS ATVGFSALSE MARTLEHALE HVRWQPHGVP EQAATFVATA
EDIRRLLHQF AAGFLKEPNP QLMDELRAIL HTEAEMASAD SGAEPEAPEA AWAEQEPQEG
LADAPPPPAP STAQDIDDEI DARDVIDPDL FPIFEEEAAE LLPGLGAALR QWVARPGNLG
ARNELLRGLH TLKGSARLAG AMRLGAMAHR MESAVEQIDA EAPRSEDIEP LLTHLDGLQA
GFNALRARGA QPPQPEPSSA AAAPQAARDA ATEPAAEGLP AAPAPRSTPP AAMPPRAAGP
TVRVRAQLLD RLVNQAGEVM IARSRLDARV GQMRTSLGEL SGNLERLRQQ LRDIEVQAET
QMQSRLALSK DAGAGFDPLE FDRFTRVQEL TRMMAESVND VATVQRNLQR TVEAAEDDLI
AQGRQARELQ RDLLRTRMVE FDGIAERLYA VVRQASKEAG KQIKLDIEGG SIEMDRGVLD
RMAPAFEHLL RNSVAHGIEP PEQRVAAGKP AVGRIAIALR QEGNDVAVDF SDDGAGLDLE
RIRARAVAQG LMAEGAELAP GAAAQLIFQP GFSTAAGLTE LSGRGIGMDV VRSEVQALGG
RIETQSRTGE GTSFRMVLPL TTAVTQVVML RAGHQTIGVP ASLVEIVRRT TAAELDASYA
GSQFHDGVES IPFFWLGALL QSSPRSGEPG SKTRPVVVLR SAAQRIAMHV DEVLGNQEVV
VKNLGPQLSR LPGLAGMSVL ASGAVVLIYN PVALATVYGD QARALAQAGG EPAGAASAGG
IAELAAPAAG SAGVPLVLVV DDSITVRRVT QRLLQREGYR VALASDGLQA LERLQQERPA
LVLSDIEMPR MDGFDLARNI RGDALLRDLP IVMITSRIAR KHREHAMELG VNHYLGKPYS
DEELLGLVEH YARKAELTQE EA
//
