ID Q9L3K7_BACCE Unreviewed; 672 AA.
AC Q9L3K7;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 111.
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:CAB75698.1};
OS Bacillus cereus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396 {ECO:0000313|EMBL:CAB75698.1};
RN [1] {ECO:0000313|EMBL:CAB75698.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10987 {ECO:0000313|EMBL:CAB75698.1};
RA Celandroni F., Ghelardi E., Pastore M., Kolstoe A.B., Senesi S.;
RT "Characterization of the chemotaxis genes fliY and cheAin Bacillus
RT cereus.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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; AJ272331; CAB75698.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L3K7; -.
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 Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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: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 Pfam; PF07194; P2; 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 Kinase {ECO:0000313|EMBL:CAB75698.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 286..536
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 538..672
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 265..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 672 AA; 75061 MW; 61B86FFD952555E4 CRC64;
MKMQTDLLNI FFEESEEHLQ SLNENVLTLE QNPTDMDVVG EIFRSAHTFK GMSASMEFTE
MADLTHKMEN VLDEIRHGNI VVHANIIDVI FECIDNLEKM VADVQQGGMG NIDVVATKQK
LEALLNGNAE TSMEHVEQES INNDDAVSHE VHITVEQQAI LKAVRAIMCI EALQNIGDIQ
KTVPSIEEIE ADAFGFEFTV FMNTDRSEQE LKQVVLHVSE IEKVVVKQGE SLQEVDSMVA
TQETTRVEEM IQPSVVAQVE APIETAKQPA STTPTKSTAK TKNAKGENRS IRVQLEKIER
LMNMFEESVI ERGRIDELAQ AIQSKELIEH LNRLGDISKD IQNVLLNMRM VPIETVFNRF
PRMVRMLAKD LGKKIDLQIT GEDTEVDKIV IDEIGDPLVH LIRNAIDHGI ETVEKRRDAG
KNETGTIKLE AFHSGNHVVI QITDDGNGIH KGKEFVKAIK NGVVTESEAN KLTDREVFDL
IFQPGFSTAE VVSDLSGRGV GLDVVKHTIH SLGGHLIIDS EEGKGSTFRI ELPLTLSIIQ
SMLVQTNDKR YALPLGNIVE AIRIKREDIQ SIQGKDVLNY RDQIIEVKHL STVFGEKTVD
EAFESYESQM VPVLIVRNTH RSYGLIVNTI IGQREIVLKS LGDFFAESSN YFSGATILGD
GRVVLILNPE GL
//
