ID A0A494XDE8_9BURK Unreviewed; 744 AA.
AC A0A494XDE8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:RKP45623.1};
GN ORFNames=D7S89_20025 {ECO:0000313|EMBL:RKP45623.1};
OS Trinickia fusca.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP45623.1, ECO:0000313|Proteomes:UP000280434};
RN [1] {ECO:0000313|EMBL:RKP45623.1, ECO:0000313|Proteomes:UP000280434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP45623.1,
RC ECO:0000313|Proteomes:UP000280434};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL Submitted (OCT-2018) 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 -!- 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:RKP45623.1}.
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DR EMBL; RBZV01000009; RKP45623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XDE8; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000280434; 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 Reference proteome {ECO:0000313|Proteomes:UP000280434};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 391..599
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 601..736
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 257..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..417
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 744 AA; 77817 MW; A5317652FF19C779 CRC64;
MTLDITQFYQ TFFDEADELL AQMEQLLLNL DVGTPDPEDL AAIFRAAHSI KGGAATFGFT
ALTETTHILE SLLDRARNNE LTLRKDMIDT FLETKDVLAD QLTAYRASEE PDGAAAAAIC
AKLERLRDGG AAPAAAAPAP APAPAAAPVP AAVVESDGVT APEHVVAQAV EATHGDAPAQ
AGGADSNAGP HLKITLRGVG EKDQALLTEE LGNLGHIVGQ VKNGSDLVVY LESEVPTDDI
TAVCCFVIDE SQISIGRGTA PGEHAQAADE PAASAQPASA PAAASAPSAP AAASAAQAPA
ASAQAAVVAE PAESAPAAAA TAASAPAAKP AAAGDDKKAA RPAAAAAGGE GSSIRVGVEK
VDQLINLVGE LVITQAMLAE TTSTFDPALH DRLFNGMAQL ERNARDLQEA VMSIRMMPMD
YVFSRFPRLV RDLAAKLGKD VELVTFGQAT ELDKSLIERI IDPLTHLVRN SLDHGIETVE
VRRAAGKDGT GQLVLSAAHH GGNIVIEVSD DGAGLRRDKI LAKAIKQGMQ VSESMTDEDV
WNLIFMPGFS TAEQVTDVSG RGVGMDVVKR NIQSMGGHVE ITSHAGKGTT TRIILPLTLA
ILDGMSVKIG NEIFILPLNF VMESLQPSAD DIYTVANGER VVRVRGEYLP LVALHEAFSV
DGARTDPTQG IVTIMQTEGR RFAMLIDELV GQQQVVVKNL ETNYRKVRGI SAATILGDGS
VALIVDVAAL NRESRVTHGA MNFS
//
