ID A0A1W9K5Y9_9PROT Unreviewed; 692 AA.
AC A0A1W9K5Y9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BVN35_01620 {ECO:0000313|EMBL:OQW79562.1};
OS Proteobacteria bacterium ST_bin11.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978759 {ECO:0000313|EMBL:OQW79562.1, ECO:0000313|Proteomes:UP000192691};
RN [1] {ECO:0000313|EMBL:OQW79562.1, ECO:0000313|Proteomes:UP000192691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin11 {ECO:0000313|EMBL:OQW79562.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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 -!- 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:OQW79562.1}.
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DR EMBL; MSXO01000003; OQW79562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9K5Y9; -.
DR STRING; 1978759.BVN35_01620; -.
DR Proteomes; UP000192691; 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: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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 340..554
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 556..692
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 274..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 692 AA; 75469 MW; AA1596B1C5F618C6 CRC64;
MSIDMAQFHQ VFFEESFEGL DAMESGLLNL DLGDVNVEDI NTIFRAAHSI KGGSETFGFS
AVSDFTHVME TLLDEMRDGR RKVTQPAVDV LLGSVDCLRD MLQSIQNGSE VDQADVAEHK
LALDSELNNA AANSPAAGKP ISKVSDALPV DDVKQIAGWV IAFSPHLHLL KTGNEPVRMF
RELASLGALT TTVDLQGVPD LYDFDPEECH LSWKLEISGD IPEAEIDEIF DWVEDDCDLA
KQPVYRIAQP LLQVPSSAAV AITPVADRIN ADLGSELASN EESESNQLDR KTGKKEDAKA
APKGSSSIRV DTSKIDTLIN MVGELVITQS MLSLLGEHFE LNRLDQLKNG LSQLERHTRE
LQESVMNIRM LPISFVFSRF PRLAHDISSK LGKKIELKLV GENTEVDKTV VELLSDPLVH
LVRNSLDHGI EMPDVRLAAG KPETGTVTLE AYHRGGNIVI EVADDGKGLD RDKLRAKAIE
KGLIDADAIL SDKQTYELIF MPGFSTAEKL TDISGRGVGM DVVRRNIQAL GGNIEILSEL
GKGSTISIHL PLTLAILDGQ SIAVGDETYI LPLGSIIESL HVKEDRLNRV AGKGETFLLR
GQYLPIIRMH QIFSVLTAKT TKLTEGLIVV VEGQGMRCGL FVDDLLGQQQ VVIKSLEANY
RRIEGVSGAT ILGDGSVALI LDIPGLVRLA NQ
//
