ID A0A1E5X662_9PSED Unreviewed; 776 AA.
AC A0A1E5X662;
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=AX279_20220 {ECO:0000313|EMBL:OEO24150.1};
OS Pseudomonas sp. J237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1904754 {ECO:0000313|EMBL:OEO24150.1, ECO:0000313|Proteomes:UP000095383};
RN [1] {ECO:0000313|EMBL:OEO24150.1, ECO:0000313|Proteomes:UP000095383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J237 {ECO:0000313|EMBL:OEO24150.1,
RC ECO:0000313|Proteomes:UP000095383};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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:OEO24150.1}.
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DR EMBL; MKEP01000031; OEO24150.1; -; Genomic_DNA.
DR RefSeq; WP_069901771.1; NZ_MKEP01000031.1.
DR AlphaFoldDB; A0A1E5X662; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000095383; 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 Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 429..638
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 640..774
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 776 AA; 82216 MW; 7A830D8441BC7E29 CRC64;
MSFGADEEIL QDFLVEAGEI LEQLSEQLVE LESRPDDMNL LNAIFRGFHT VKGGAGFLQL
NALVECCHIA ENVFDILRKG ERRVDSELMD VVLEALDTVN AMFDQVREGA ELTPATPELL
AALANLAQPQ ELLSEEAPAP VTEHVVAGNP VAASAVTDNP AAADDAAADD VAGTPAAADA
VIADDEFEQL LSALADNAAQ AQKAPASPVA SAAQPSDSDE ITDDEFESLL DQLHGKGQFV
ANAGGQPVKA QQDDDVAVAD APDEITDDEF EALLDQLHGK GQFASGAAPA LAATATAATG
LPASTPSEPV APVAASSAAS ADEINDDEFE ALLDELHGKG KFSETPAVSA APVAAKAVEK
PAAKPAAKPV AAAPAKAPAP EKAAPVNEAE TTVRVDTARL DEIMNMVGEL VLVRNRLVRL
GSTSSDEAMA KAVSNLDVVT ADLQSAVMKT RMQPIKKVFG RFPRLVRDLA RSLKKEISLE
LIGEETDLDK NLVEALADPL VHLVRNAVDH GIETPEERVA AGKSRGGKVV LSAEQEGDHI
LLVISDDGKG MDADVLRRKA VEKGLLEKEA ADRLNEFECY NLIFAPGFST KTEISDVSGR
GVGMDVVKTK ISQLNGTVNV FSVKGQGSRI VIKVPLTLAI MPTLMVMLAN QAFAFPLVNV
NEIFHLDLSR TNVVDGQEMV IVRDKALPLF YLKRWLVGQA AHEEQVEGHV VILTVGNQRV
GFVVDQLVGQ EEVVIKPLGK MLQGTPGISG ATITGDGRIA LILDVPSMLK RYARRS
//
