ID A0A0J1CQH3_9BURK Unreviewed; 756 AA.
AC A0A0J1CQH3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EOS_28270 {ECO:0000313|EMBL:KLU22902.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22902.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU22902.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KLU22902.1}.
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DR EMBL; AEJF01000171; KLU22902.1; -; Genomic_DNA.
DR RefSeq; WP_047895494.1; NZ_AEJF01000171.1.
DR AlphaFoldDB; A0A0J1CQH3; -.
DR PATRIC; fig|908627.4.peg.6323; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000035963; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.70.400; CheY-binding domain of CheA; 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; IPR015162; CheY-binding.
DR InterPro; IPR035891; CheY-binding_CheA.
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; PF09078; CheY-binding; 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; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 404..612
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 614..749
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 296..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..430
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 756 AA; 80902 MW; 77B85AD28B60E7E5 CRC64;
MTLDITQFYQ TFFDEADELL ADMEQLLLAL DLANPDPEDL GAIFRAAHSI KGGAATFGFS
ALTETTHILE SLLDRARNNE LVLRRDMIDT FLETKDVLSD QLGAYRASAE PDAVAAKAIC
AKLEYLRDND PADEVSAIAG TTDMAEPEPE QSFPDTAALA QDLAQVALAL GPNEPPPHVI
EQASEAVEED GEWTEFPVAP DASHVADNAA EQDGPHLKIT LRGVGEKDQA LLTEELGNLG
TVVGERKSGA DLTLWLDSDV SSDDIVAVCC FVIDEAQIAV SRGNAADAAP AGASQAAAEL
EESTEVAAVA PASEKTEPVA APAAAESRTN TGTSTAVTEV PEAPKAPEGD KKTRAGAAPA
AAEGSSIRVG VEKVDQLINL VGELVITQAM LAETTSTFDP ALHDRLFNGM AQLERNARDL
QEAVMSIRMM PMDYVFSRFP RLVRDLAAKL GKEVELVTFG QATELDKSLI ERIIDPLTHL
VRNSLDHGIE TVEARRAAGK AAVGQLVLSA AHHGGNIVIE VSDDGAGLRR DKILAKAMKQ
GMQVNEQMSD DEVWQLIFMP GFSTAEQVTD ISGRGVGMDV VKRNIQAMGG HVEIQSREGK
GTTTRIVLPL TLAILDGMSV KVGNEIFILP LNFVMESLQP VSDDIYTVAG GERVVRVRGE
YLPLVALHQV FEVTDARTEP TQGIITIIQS EGRRFAMLID ELVGQQQVVV KNLETNYRKV
HGISAATILG DGSVALIVDV AALNRETRSA HGALTH
//
