ID A0A2D2B1P1_9CAUL Unreviewed; 750 AA.
AC A0A2D2B1P1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CSW64_18250 {ECO:0000313|EMBL:ATQ44189.1};
OS Caulobacter mirabilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69666 {ECO:0000313|EMBL:ATQ44189.1, ECO:0000313|Proteomes:UP000228945};
RN [1] {ECO:0000313|EMBL:ATQ44189.1, ECO:0000313|Proteomes:UP000228945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FWC 38 {ECO:0000313|EMBL:ATQ44189.1,
RC ECO:0000313|Proteomes:UP000228945};
RA Fiebig A., Crosson S.;
RT "Genome sequence of Caulobacter mirabilis FWC38.";
RL Submitted (OCT-2017) 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; CP024201; ATQ44189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D2B1P1; -.
DR KEGG; cmb:CSW64_18250; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000228945; Chromosome.
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:UP000228945}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 392..595
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 597..733
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 303..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 750 AA; 78469 MW; 282BABA3CFB2A43D CRC64;
MDPMDAIRTT FFIECDELLA QLEEGLMAME QGATDSETIN SVFRAVHSVK GGGGAFGLDP
LVRFSHVFET LLDQIRSGQV DPSETVVATL LRAADMLADH VNAARDGGVA DEARSEQIAA
AIMALTVGGA ANAFEEQPAE IEGLNFTPQL VSLDLPAAAP ADDFDLAALL ASAGVDAPAA
EAADGDWLVT FAPHASLYAK ANDAALVLRE LIGLADEATV SLDDEALLPL EEMDPAGAYL
GWTVRLPASV AEADIRDAFA FVDEDCDLEI KREGGAADTV AVEPQAEESL NLLDSLLLQV
KEEPAPDPHP APAAPAAAVD PAPKPEAVAA GAPMQAAASA TAAAPPQTIR VDLDRVDRLI
NLVGELVINQ AMLAQRVHES GAGKATDVNL ALTDLELLTR GIQDSVMAIR AQPVKSVFQR
MPRLVREVGE ATGKRVRLVT EGEGTEVDKT VVEKLSDPIT HMIRNAIDHG LETPAEREAA
GKSAEGTVRL TAAHRSGRIV IEVADDGKGV DRVRVKAKAI EKGLIATDAQ LSDEEIDNLI
FAPGFSTAST VSDISGRGVG MDVVKRSVQA LGGRITIVST PGQGSRFSLS LPLTLAVLDG
MVVTVGDQTL VAPLTAIIES LKPRAGEVRP LGPHNKVLQI RDAYVPLIDT GAALGFGRSA
LEPTEGVALL VDSENAGQVA LMVDQILGQR QVVIKSLETN YGATDGVAAA TILGDGRVAL
ILDIDGLVTA HRRMPPPAPR TESLVLTAAE
//
