ID A0A1Y5TNW0_9RHOB Unreviewed; 800 AA.
AC A0A1Y5TNW0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JAN-2026, entry version 27.
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:SLN64796.1};
GN ORFNames=AQS8620_02972 {ECO:0000313|EMBL:SLN64796.1};
OS Aquimixticola soesokkakensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Aquimixticola.
OX NCBI_TaxID=1519096 {ECO:0000313|EMBL:SLN64796.1, ECO:0000313|Proteomes:UP000193862};
RN [1] {ECO:0000313|EMBL:SLN64796.1, ECO:0000313|Proteomes:UP000193862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8620 {ECO:0000313|EMBL:SLN64796.1,
RC ECO:0000313|Proteomes:UP000193862};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWFS01000012; SLN64796.1; -; Genomic_DNA.
DR RefSeq; WP_085837782.1; NZ_FWFS01000012.1.
DR AlphaFoldDB; A0A1Y5TNW0; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000193862; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 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; IPR051315; Bact_Chemotaxis_CheA.
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; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000193862};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLN64796.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 446..649
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 651..787
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..384
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 800 AA; 84278 MW; 92067C89C663130D CRC64;
MSDPMAEIRA SFFIECEELL ESLQDGLQMM DDGESDSETI NIVFRAVHSI KGGAGAFGLN
DLVHFAHRFE TAMDEVRTGR FVPDGEAIKI FFACADVLGD LVRASRDETP ILDEMTAPVL
DSLERLVGME EEVEEEVEFV PAGIALDLGG LGDLGGGMGD LPPLDLPALD MPSPDLLSAD
GLPEGSETPD VAGDNDAQAA LGKGFKIHFL PEPALFISGN EPLYLFRALR DLGDLTVRCD
TSRLPAAEAL AAETGYLSWS LVLLTEEPET AVRDVFEFVD GLCVLTIEPI TNAALDGSMA
LPDLDVPSAQ IPLAPGDSAE TAPVETIAAE APPSSPAQAA PAALPDRLAP GAAAAPIPAP
IPAPAAAPVA PPAPIESAAE STEPSDAPSR EAKNAPTQPR ATVRVDLERV DRLVNLVGEL
VINQAMLSQS VTEAGLPANS AVSTGLEEFL QLTRDIQESV MMIRAQPIKS LFQRMGRIVR
EASAAVNKDV RLHTDGENTE VDKTVIERLA DPLTHMIRNA VDHGLETTEK RVASGKPRNG
HVTLTAQHRS GRIVIDVSDD GGGINRPRVL EKAIEKGLVS PEAQLSDGEI DNLLFLPGFS
TAAEVSALSG RGVGMDVVKS SIQSLGGRIA ITSVEGKGTT FSISLPLTLA VLDGMVVRVA
GETLVVPLNA ILETLTLTDD DIKQLGPETH VVQLRGGFVP LLDLGAELGY RTPEQSYVGG
IVLLIGQEDG HRAALVVDAI EDQRQVVIKG LEGSYGRVPG IAAATILGDG QIALILDPMD
LISQASGRTK DRSLSLSHAG
//
