ID D0IC81_GRIHO Unreviewed; 716 AA.
AC D0IC81;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
GN ORFNames=VHA_003360 {ECO:0000313|EMBL:EEY71499.1};
OS Grimontia hollisae CIP 101886.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY71499.1, ECO:0000313|Proteomes:UP000003604};
RN [1] {ECO:0000313|EMBL:EEY71499.1, ECO:0000313|Proteomes:UP000003604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY71499.1,
RC ECO:0000313|Proteomes:UP000003604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (OCT-2009) 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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:EEY71499.1}.
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DR EMBL; ADAQ01000013; EEY71499.1; -; Genomic_DNA.
DR RefSeq; WP_005506642.1; NZ_ADAQ01000013.1.
DR AlphaFoldDB; D0IC81; -.
DR GeneID; 58895314; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000003604; 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 PANTHER; PTHR43395:SF1; 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:UP000003604};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 368..579
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 581..715
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 127..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 716 AA; 76736 MW; 96E9C5489DDAFF37 CRC64;
MSFEMDEEIL QDFLIEAGEI LELLSEQLVD LEKTPDDRDL LNAIFRGFHT VKGGAGFLSL
TELVETCHGA ENIFDNLRNG GRELTSEVMD TILQALDTVN EQFACVQERE AVPAAEPSLI
EALHKYSRPA SEDEDTEAAA PEPEPEPEPE PVDEATAEGE EAIAGDSVDD ITDDEFDRLL
DELHGAGKGP QAGDSTSTPS VDAASSGGDD ITDDEFEKLL DDLHGTGKGP QAGDAATPPP
QNVSVESPDS DEITDDEFEK LLDDLHGKGK SPIASEASKT APEPPKTPAP KVEPKPAPAP
KAEPAAAKPP AAVAKPPAKA DDKKPPAPQV EQTVRVNTST LDTIMNMVGE LVLVRNRLVS
LGANSDDENM AKAVTNLDVV TADLQGAVMQ TRMQPIKKVF GRFPRVVRDL ARSLKKDIVL
EMRGEETDLD KNLVEALADP MVHLVRNSVD HGIEMPDVRE QKGKPRTGTI TLAASQEGDH
ILLTIEDDGG GMDADKLRSI AVNRGVMDAD AAARLSDTEA YNLIFAAGFS TKTEISDISG
RGVGMDVVKT AITQLNGTIS IDSELGRGTI ISIKVPLTLA ILPTLMVGIG NNPYAFPLSN
VNEIISLDLS KTNTVDGQLT LIVREKAIPL FYLQDWLCPR RGIANREVGH VVIIQMGHQP
VAFVVDSLIG QEEVVIKPLD ELLQGTPGMA GATITSDGHI ALILDVPNLL KRYAGR
//
