ID A0A1H9ATY6_9GAMM Unreviewed; 879 AA.
AC A0A1H9ATY6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421693_10650 {ECO:0000313|EMBL:SEP79388.1};
OS Ectothiorhodospira magna.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=867345 {ECO:0000313|EMBL:SEP79388.1, ECO:0000313|Proteomes:UP000199496};
RN [1] {ECO:0000313|EMBL:SEP79388.1, ECO:0000313|Proteomes:UP000199496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7-7 {ECO:0000313|EMBL:SEP79388.1,
RC ECO:0000313|Proteomes:UP000199496};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOFO01000006; SEP79388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9ATY6; -.
DR STRING; 867345.SAMN05421693_10650; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199496; 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; 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 Kinase {ECO:0000313|EMBL:SEP79388.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000199496};
KW Transferase {ECO:0000313|EMBL:SEP79388.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 544..746
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 748..879
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 138..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 879 AA; 95128 MW; 01BCCE8CB45548FA CRC64;
MNPLLDQFIS ESRDAIQAIG ERLLQLENAP DDLELMDELF RLVHTLKGNS GLFDFPEMTR
VLHGAEDLMD AVRDRRIGYS QTLADQLLEA MDFVSALLDE ILAAGSTSLP ANGDRGSDAV
ALTQALRQLI PVPDDAADAA NATDATNPDP QAPPTATGEE TPSPLMGVPE AARMAAYKQV
AAGQPCTWLR YEPEEECFFK GEDPFYQMIQ LPAPLWQQVS AREPWATPEN LDAYRCLLRF
ECIIPLGPEP LAEHFRYVPD QVTLLPLTPE ALAVPVGDDD HDGVPIEEYL KTAMGHLEAG
QREGLIQASR VMLELASPRL RMASALRWLV LALETCPEDG TLPRTLLTAL GPKTAPPPAP
AAGEAPATAD MPPILRDILQ AQAEILALED TPPWLAGRLR AVAASLRAAF TQLGQPELLD
GLDNALAEAL TAEASTPLAL WLAERMPKTA TPPAPASQPA PQGNGSNGGN GNGREPRKFG
RRVEDTYAGP SAIKVDQAKI DRLMNLIGEM IVAKNALPYL AARAEEVFGV RELAREIKGQ
YGTLNRIADE MQDAIMQVRL LPVSFVFQRF PRLVRDTAHK LGKEVRLVME GESTEADKNV
IESLADPLVH ILRNSLDHGL ETPEERRAAG KPAAGRLTIS ARSESDRVVI EITDDGRGID
PEAIRRKAYE KGIIDEQALE RMTEQEALNL IFAPGFSTAT QVSNLSGRGV GMDVVRTAVA
RVNGSIDLKS RPGQGTRLRL SLPLSMAVTN VMVIVSAGQR FGVAMDAVAE TVRVAQAHIQ
LIKHRMTTVL RGRVVPLVTL NDLLALNQPQ IPNEDGELAV VVVRIDGDFV GIIVDDCRET
VDIILKPLAG FLGDLGGYAG SALLGDGSVL LVLNPRELL
//
