ID A0A1E4HHE5_9GAMM Unreviewed; 1954 AA.
AC A0A1E4HHE5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ABS82_06445 {ECO:0000313|EMBL:ODT95983.1};
OS Rhodanobacter sp. SCN 67-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1660133 {ECO:0000313|EMBL:ODT95983.1, ECO:0000313|Proteomes:UP000094158};
RN [1] {ECO:0000313|EMBL:ODT95983.1, ECO:0000313|Proteomes:UP000094158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(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:ODT95983.1}.
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DR EMBL; MEFB01000029; ODT95983.1; -; Genomic_DNA.
DR Proteomes; UP000094158; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ODT95983.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:ODT95983.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 678..785
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 871..975
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1165..1268
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1430..1663
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1665..1802
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1828..1944
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1023..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1362..1396
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 725
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 915
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1212
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1877
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1954 AA; 212143 MW; CC3B0DD5F7A4D25A CRC64;
MRLQDHIDFT TLQWVKPELD DTLSIAREAL ESYVDNPGKR DFMRTCTDHL HQVHGTLKMV
ELYGAAAVTA EMEALVGALL NDQVLQREEA YAALMRGLMQ LPDYLERLSS GHRDVPVVLL
PLLNDLRATR GLEPLPESSM FHPNLDAFLP EQAPAAMSEA YAAAHRVELA GLRLRFQQQL
LAWFRGQDAA QQLVAMRKTL LAITARCYHV HGRRLWWIAA GVLEGLEQGM LKGHAPEVRQ
LIGKVDRNIR LLIEHGENSL RASDADEVAC KLLYIVAQAK QRSPHMELLR STYALDSLLP
DAGELEHARG SMAGHNRALL DSVSRALKDD LLRVKEALDL FLREQDGDPA QLAAQGEVLE
RVGDTLGMLA LAVPRRVVGE QRRVLDEIAN RLRPADEETL LDVAGALLYV EASLDDHIES
LGSEGEPAAA ADPTQGLPRS EALGVVSTLM QEAIGNTGKV KDAIVAFVES GWQHDRLAGA
PPLMDEVAGA MRMLSSPRPA ELAQGVGRFI DYELLQDRRV PSGAQMDHLA DALAALEYYL
EAAREHRGGL EHILDVAEHS LAQLGYWPVP AQRAAVEEPA PVAEAPASVS LEAEQHPDLS
ESVSLLPGAD LGSLFVGDAQ ASPEPTHDLD GLRLAETGAP ASPASAVGED WVEIEEQVTE
QVPVADPLSA NTRFNADAEG IDDDIRDIFL EEMQEEIDNL AVAQKDWLAD PAQTPALVGI
RRSFHTLKGS GRLVGAGVLG EFAWKVEDML NRVLDHTIEP DQNVQDVVRH AIDALPQLLA
ALKGEGDPQV PLSAIMQAAE RLAAGQPARV EDFMQRGTET VTRTVVRRVP RATVDAADVP
RASLTDADVA SAAAAEPVPA EPEPLVDMPA MPPIDPVLLE ILRSEVAQYL QTIRTAIQRS
EGALPVSEEL LRAVHTLHGA IAMVDIPLLT QLLSPLEGLF KRLRASGQPL PASGVRLLGQ
AADVVDQVMA QFDAPALPLP NVDALTAQIT EMRDDYPESQ VAHVIFEPQA GDDAVDEPAI
EADTARESTP TLAEPSAPEG VDAETGHDEH MDAAAEMTAA LRAFEPDAAI AAANAAAEAA
RQAAAEQAAA EQAAQEEAAR ERAAAEQAAA EQAAAEQAEQ LAAAQAAAEQ AAAEQAAAEQ
AAKQAAARAA ATRVEPAPAF VLPDGSRIDA DLLEVFIDEA REILDSADGV LAKWHADPAD
TSCVGELQRD LHTLKGGARI AGLVSVGDLA HAIETVLEKP IRDADKTGTL ISALEASFDQ
LNTMVQRVSQ GHMPEYPQAA IDHLLQLAGA TALVGEAEPA TDASHAPVEE APQPVAHEDE
HSLPELLPET ARETHSPQEQ IRVRADLLDN LVNHAGEVAI YRSRLEQQVA GYRFNLVELE
QTVARLRSQL RMLEIETEAQ IIARFQREHR EAGLTAFDPL ELDRYSQLQQ YSRALAESVS
DLVSIQNMLD ELTRQAETLL IQQSRVSTEL QDGLLRTRML PFDTMVPNLR RTLRQAAQEE
HKQAQLYVDG AHGEMDRNLL DRIKAPFEHM LRNAIAHGIE SPAERRKLGK PAEGAVRIKV
AREATEVVVR VSDDGRGLNR EAIRKRGIER GMLRPETRPT DNQLLSLITQ PGFSTASQVT
QLAGRGVGMD VVANEIKQLG GSLSIESEEG QGTTFVLRLP FTLAVTQAIL VRIGEATFAI
PMTSVQGVAR VNPEDLAALL ATDEPSFQYG NEDYGVHDLA ELLGLPPGLA TEDEQQPLLL
TRAGDLRAAI RIDAVLGSRE IVVKSVGPQI SSVPGLLGAT IMGDGSVLII LDLAPLVRHG
MIRREQRLAE GLSAVKAPVI EEVLVRPLVM VVDDSITMRK VTGRVLERHE YEVSTAKDGV
DALEKLHERV PDLMLLDIEM PRMDGYELAT HMKADPRLRD VPIIMITSRS GDKHRQRAFD
IGVDRYLGKP YQEAELLLQI AEVLEQRAAE PIHD
//
