ID A0A0W7Z5R7_9BURK Unreviewed; 716 AA.
AC A0A0W7Z5R7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AS359_12445 {ECO:0000313|EMBL:KUF42491.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF42491.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF42491.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF42491.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-2015) 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:KUF42491.1}.
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DR EMBL; LPXH01000014; KUF42491.1; -; Genomic_DNA.
DR RefSeq; WP_058879509.1; NZ_LPXH01000014.1.
DR AlphaFoldDB; A0A0W7Z5R7; -.
DR STRING; 225992.B5M06_04155; -.
DR Proteomes; UP000053300; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000053300};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 11..115
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 372..580
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 582..716
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..92
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 147..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 716 AA; 76130 MW; 47489CF428C9E683 CRC64;
MADTHQGGAE ADFDLTQFYQ IFFEEAAENL DQMEQMLLNL DLNAANDEEL NGIFRCAHSI
KGGSATFGFT DVAELTHKME SLLDRLRRHE ITPVPEMVDV LLEASDAARS LLARHQAGGE
GEALPTEDLV SRIARLAAGE GAAPAAAPAP APQPAPAPEP VPAPAPTPAP EVVAAPAAAP
AAGGVRHLQI KIGPVENLET ADAIKELFRD IPGLGSIKDL PCEEPKSRLF EVETQSTDDD
LLDLMAFHVT KEQVQISPVG AAAPAAQAAA SEPAEVAQAP AEAKDEATAP AVALPESEAF
GIFDGAPGAP VNKPVAAAVK TVTRPNIAQM ESTSIRVDVK KVDQLINLAG ELVIIQAMLA
QNSRALDPST NQQLLAGLAD LDRNTRDLQE AVMSIRMIPM STVFSRFPRM LRDLANKMGK
KINLVTQGEA TELDKGLVEK ITDPLTHLVR NSVDHGIESP EDRLAAGKPE AGTLTLSASH
QGGSIVIEVR DDGKGMNREK ILKKARERGM DVSDSMPDGE VWQLIFAPGF STADVVTDVS
GRGVGMDVVR KNIAALNGSV EIDSVQGVGM RVSIRLPLTL AIMDGMSVGV GNEVYILPLS
SVVESFQVNP ADVSTVTQGA QLVKVRDEYM PVIELEKVFG VPRHGDGKRS DIMVVIESDG
MRVALLVDEL LGQHQVVVKN LESNYRKVPN VSGATILGDG TVALILDTSS LVRRAR
//