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Database: UniProt
Entry: W6M4F8_9GAMM
LinkDB: W6M4F8_9GAMM
Original site: W6M4F8_9GAMM 
ID   W6M4F8_9GAMM            Unreviewed;       681 AA.
AC   W6M4F8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cheA {ECO:0000313|EMBL:CDI02562.1};
GN   ORFNames=BN873_330039 {ECO:0000313|EMBL:CDI02562.1};
OS   Candidatus Competibacter denitrificans Run_A_D11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria;
OC   Candidatus Competibacteraceae; Competibacter.
OX   NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI02562.1, ECO:0000313|Proteomes:UP000035760};
RN   [1] {ECO:0000313|EMBL:CDI02562.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI02562.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI02562.1, ECO:0000313|Proteomes:UP000035760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI02562.1,
RC   ECO:0000313|Proteomes:UP000035760};
RA   McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA   Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT   "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT   functional metabolic diversity.";
RL   Submitted (FEB-2014) 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:CDI02562.1}.
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DR   EMBL; CBTJ020000040; CDI02562.1; -; Genomic_DNA.
DR   RefSeq; WP_048672886.1; NZ_CBTJ020000040.1.
DR   AlphaFoldDB; W6M4F8; -.
DR   STRING; 1400863.BN873_330039; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000035760; 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   Kinase {ECO:0000313|EMBL:CDI02562.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035760};
KW   Transferase {ECO:0000313|EMBL:CDI02562.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          328..542
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          544..679
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          246..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..286
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   681 AA;  74561 MW;  20152479491637EB CRC64;
     MAIDLAQFIQ TFFEESFEGL DVMEAGLLAL EPDAAVDLEQ INTIFRAAHS IKGGSGTFGF
     KNVTDFTHLM ETLLDKMREG RMAISRAAVN TLLESVDCLR EMLVAARENA QVDDERVQAL
     RDRLMQLLEL KQTAPTATPA SDEPTPPQTL GWCIQFQPYP QMMHSGNDPV RMFRELAELG
     ELTVRPDVAR LPRLADLQPE DCYLSWELEL VGLAPHDAVA EVFAWVEGDC ELTLTPLVEA
     VTPVSAAPPL PSPAVRPGTA EEGQQGELLL ERRQTEDRRK GDRRASAVTT PDGGSIRVGI
     DKVDAVINLV GELVTTQSML SALGEGFDMS RLDKLHEALD QLDRNTRDLQ EHVMRIRMLP
     VSSVFSRFPR LVHDMSGKLG KEVDLRINGE QTELDKTVIE KIGDPLVHLI RNSLDHGLEP
     PDERVRAGKP ATGVISLDAY HKSGSIFIEV GDDGRGLNRE ALLRKGLDTG LLKAGEDYSD
     EQIYELIFHP GLSTAKQISD VSGRGVGMDV VRRNIQDVGG SIQITSQPGK GARITICLPL
     TLAILDGQLV SIGQDCYIIP LLSVIESVQI RADAVNRVAG KGEILRFRGQ PLPILRLYEL
     FGTEDAVTDL EKGLLVVVEA DGRQVGLFVD DLEGQQQISI KSLEKNFRRV SGVAGATILG
     DGRVGLILDI SGLIRVNNPV L
//
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