ID A0A0Q8R4I8_9BURK Unreviewed; 679 AA.
AC A0A0Q8R4I8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE26_29120 {ECO:0000313|EMBL:KRB90004.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB90004.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRB90004.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB90004.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB90004.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB90004.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB90004.1}.
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DR EMBL; LMIC01000026; KRB90004.1; -; Genomic_DNA.
DR RefSeq; WP_057246798.1; NZ_LMIC01000026.1.
DR AlphaFoldDB; A0A0Q8R4I8; -.
DR Proteomes; UP000051728; 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; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 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; 1.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
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 PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 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; 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; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000051728}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 342..542
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 544..671
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 679 AA; 72436 MW; B532D21FAED04A0A CRC64;
MDLDEGLQAF VTEAGELLAE MEAGLLKLGE PAAREEAVNA IFRAAHTIKG TAGLFGLDYI
VLFTHAVESV LEEVRNGAQP LDDDLLALLL ECADQIGAMV GDVERGGRGE LGERCRPQLD
ALHAYLAPAP ALGETALPPV FGAGIEAGES GFWLVSLEFG RDVFRHGMDP ASFIAYLGRL
GRIVALATVD GGLPPPEQMD PQSCYLGFEI VLETVSNAEE ISKVFEFLHD ECTLRLLPPG
SSNDDFQRLA NILPLHGDAI AGVLQASGLG SVVPQAVAAQ LAGPEAGAVA AKPNESRTIR
VDAERLGHLI TLVGELIIAS ARTQMIGSRH KDADLQDSTS ALAELVEQVR DSALQLRMVK
IGATFNRFQR VVHDVAREIG KDIRLVLSGE DVELDKTLVE RIGDPLTHLV RNAIDHGIEP
PEVRRQRGKP LQGTVFLNAF HDSGSIVIEV GDDGGGLQRE RIIATAIERG LLDAEHKVSD
SEVFGLIFEP GFSTASTVTS LSGRGVGMDV VKRNIEALRG SITIDSEAGR GTTVRVRLPL
TLAIMDCMLV TVGSSRFAIP LGTIEECVEY EREGRRGFAD LRGEVLPTVA LRQLFRLQGS
APRRESVLVV RHAGQRAGLV VDSLQGQCQA VIKPLSPVFS GISCLSGSTV LGSGDVALIL
DIPALLKQLQ ARQAGNLAA
//
