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Database: UniProt
Entry: A0A0W7WQI0_9RHOB
LinkDB: A0A0W7WQI0_9RHOB
Original site: A0A0W7WQI0_9RHOB 
ID   A0A0W7WQI0_9RHOB        Unreviewed;       710 AA.
AC   A0A0W7WQI0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AVJ23_03660 {ECO:0000313|EMBL:KUF12816.1};
OS   Pseudoponticoccus marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pseudoponticoccus.
OX   NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF12816.1, ECO:0000313|Proteomes:UP000054396};
RN   [1] {ECO:0000313|EMBL:KUF12816.1, ECO:0000313|Proteomes:UP000054396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF12816.1,
RC   ECO:0000313|Proteomes:UP000054396};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
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:KUF12816.1}.
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DR   EMBL; LPXO01000001; KUF12816.1; -; Genomic_DNA.
DR   RefSeq; WP_058860759.1; NZ_LPXO01000001.1.
DR   AlphaFoldDB; A0A0W7WQI0; -.
DR   STRING; 1685382.AVJ23_03660; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000054396; 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   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054396}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          345..555
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          557..693
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          260..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..304
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   710 AA;  76100 MW;  BD5A608ABB44F43E CRC64;
     MSGNAIRDTF FEECEELLEA LVEGLAQMEE APDDLQVVNA VFRAVHSIKG GAGAFALDRL
     VTFAHTFETV MDKVRDRDLS VDDRLMALFH RSGDMLSDLV AAARDETPLD PAAEGELIEA
     LESYLGPASE EEEFSFDAVS LDLGGDTPAS LPEIPLAKIA DSAPDGAATG PASEKTYRIR
     FTPTRALYEN GHEPLLLFDA LAELGTLCVL LDLSGLPSFD AFDPQDSCLD WTLLLTTAEP
     ETALDEVFEF VEGLCTLEIT TAPPPAPTEA ELPTPDLPQP AARPAPPAAE SAAAPPPPKP
     EARGPKPTLR VDLDRVDRLI NTVGELIINQ AMISQRIEEL DLPTVAHLTN ELEAYKLLAR
     DIQEGVMAIR AQPVKPLFQR MSRIVREASD ATGKKARLVT VGDSTEVDKT VIERLADPLT
     HMIRNAVDHG LEHPERRLER GKEAQGTIRL SASHRSGSVF IEIADDGAGL DRAAILRKAR
     EKGLVAPEVE LTNPEIDNLL FLPGFSTANQ VSNLSGRGVG MDVVKNAVQA LGGRISITSI
     PEKGTTFTIV LPLTLAVMDG FVISVAKETM VVPIASILET IRPNARDTHV IGTSSEVVKI
     RGSYVPIVDV AANLGLDAGD ADRGGSILLL VSTETQGLTA LRVTGIHDQR QVVIKSLESN
     YAAIPGVSAA TILGDGKIAL ILDPDELIKL SRLSEPEGTE TKLMPEPGHV
//
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