ID A0A1E8CI05_9GAMM Unreviewed; 729 AA.
AC A0A1E8CI05;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PHACT_01805 {ECO:0000313|EMBL:OFE12028.1};
OS Pseudohongiella acticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1524254 {ECO:0000313|EMBL:OFE12028.1, ECO:0000313|Proteomes:UP000175669};
RN [1] {ECO:0000313|Proteomes:UP000175669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42131 {ECO:0000313|Proteomes:UP000175669};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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};
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:OFE12028.1}.
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DR EMBL; MASR01000001; OFE12028.1; -; Genomic_DNA.
DR RefSeq; WP_070115652.1; NZ_MASR01000001.1.
DR AlphaFoldDB; A0A1E8CI05; -.
DR STRING; 1524254.PHACT_01805; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000175669; 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:UP000175669};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 379..590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 592..729
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 183..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 729 AA; 77990 MW; 226074DC08D09C2F CRC64;
MSFFDDEEIL EDFLVEAGEI LEQLSEQLVQ LEKQPEDKDL LNAIFRGFHT VKGGAGFLQL
TPMVDCCHVT ENLFDNLRNG KRQVTSELMD IVLQALDCVN NMFAQIKERV PPEPASDELL
EALQMLANGD DLEPAAASPD ASVVAQVTAP QDAKLSAEAS AGDDMTDEEF DQLLAALDSA
DFEAEAENRA SESTTAPDQG AGGDEISDDE FEALLDQLQG APNASAAGKE PSADKEPSAQ
KEPSAKKEPS ADKAPSADKA PSADASNPNN DEITDDEFEA LLDQLHGGKS SDTAPEPAST
PEPVQPAAQP KPTLKAVPTT GSKPATKPET KTPAADQAPA AETTVRVDTR RLDDIMNMVG
ELVLVRNRLV RIGSTAADEM LSKAVANLDL VTADLQSSVM KTRMQPIKKV FGRFPRVVRD
LARSLKKEVT LELHGEDTDL DKNLVEALAD PLVHLVRNAV DHGIELPDKR AAGGKPRQGT
ILLAAEQEGD HILLTISDDG NGMDPDVLRG KAVEKGIMDK DAADRLSNSE CFDLIFAPGF
STKTEVSDVS GRGVGMDVVK TKITQLNGSV FIDSKPGEGT RIEIKVPLTL AIMPTLMILV
GEQAFALPLA SVSEIFNLDL NGTHVVDGQQ VVTVRDKALP LFHLRRWLTQ DMPQSAGEQK
TDANVVIVSV GAQRVGFVVD TLIGQEEVVI KPLGRMLHGT PGMAGATITG DGRIAVILDV
PGLLKRYAA
//
