ID G2E7T1_9GAMM Unreviewed; 709 AA.
AC G2E7T1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ThidrDRAFT_4344 {ECO:0000313|EMBL:EGV27842.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV27842.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV27842.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV27842.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) 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:EGV27842.1}.
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DR EMBL; AFWT01000056; EGV27842.1; -; Genomic_DNA.
DR RefSeq; WP_007043057.1; NZ_AFWT01000056.1.
DR AlphaFoldDB; G2E7T1; -.
DR STRING; 765913.ThidrDRAFT_4344; -.
DR PATRIC; fig|765913.3.peg.4418; -.
DR eggNOG; COG0643; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000004200; 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 InterPro; IPR037257; T2SS_E_N_sf.
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; SSF160246; EspE N-terminal domain-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 Kinase {ECO:0000313|EMBL:EGV27842.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:EGV27842.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 309..557
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 559..691
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 709 AA; 77600 MW; 631B9F3A5C713156 CRC64;
MSDPVDIFRT EAEEHLSALE SALLELEQRP EDPELIALAF RAMHTIKGGG GMFGFTELSA
FTHHLETALD KVRNGLFPVS PELISILLDA KDHIMGLLED PVLDQTQILV GRGLLERLHA
LIPDEQITEA KQTTAAQSTA IADPGGEGRD QVYRVRIRPS AGAFRDGFDI FPILKELQGL
GTCYITTDTG GVPVLAELDP ESCMLSWDLV LVTSQGVEAI RDTFIFVADE WRIDIDPIDI
DDDQCDRIGE ILVERGLIAR SQIETLLAEK PRVGEVLQQA GLVTETDVDA ALREQQAIRD
TRERSARGEQ ESLVRVPAAR LDSLMNLVGE LVIVQARMHQ LAQSRDDEAM GAISEDLDRL
TTELRDNTFS IRMLPIGTTF GRFRRLVRDL SRELGKEIRL ETEGAETELD KMVIDRLGDP
LVHLIRNSID HGIEPPEQRE AAGKPAAGTI HLAAEHAESH VVIRIRDDGA GLNTGAIRAK
AVERGLIARD QTLTEEEIQS LIFEAGFSTA DRVSDISGRG VGMDVVKRSI QDLGGQVGIR
SEPGRGTTLT ITLPMTLAII EGLMVAVSEE RYVLPLSCVE ECIEVERGSE GKRNGQRLAR
VRGDLVPYLS LREWFAVPGA APDIEQIVVT RLGEQRFGFS VDQVVGQYQT VVKRLGKLYE
GNAGLAGATI LGDGGVAMIL DAGALAESLE DEVRTRGRKQ TGRPPMGTK
//
