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Database: UniProt
Entry: A0A0W7Z5R7_9BURK
LinkDB: A0A0W7Z5R7_9BURK
Original site: A0A0W7Z5R7_9BURK 
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
//
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