ID A0A1M4MYN4_9RHOB Unreviewed; 669 AA.
AC A0A1M4MYN4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:SCM67682.1};
GN ORFNames=KARMA_1884 {ECO:0000313|EMBL:SCM67682.1};
OS Donghicola eburneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Donghicola.
OX NCBI_TaxID=393278 {ECO:0000313|EMBL:SCM67682.1, ECO:0000313|Proteomes:UP000184085};
RN [1] {ECO:0000313|Proteomes:UP000184085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
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};
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DR EMBL; FMJB01000047; SCM67682.1; -; Genomic_DNA.
DR RefSeq; WP_072706323.1; NZ_FOXY01000001.1.
DR AlphaFoldDB; A0A1M4MYN4; -.
DR Proteomes; UP000184085; 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:UP000184085};
KW Transferase {ECO:0000313|EMBL:SCM67682.1}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 313..521
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 523..657
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 669 AA; 71466 MW; 24B141E77D9DD921 CRC64;
MSMDALKATF FAECEELVEA MTEGLQQIGD DDWGSETVNA IFRAVHSIKG SAGAFGFETL
VAFAHRYETV LDKIRSNTLG IDADVLRVIT RASDVLAELV ELAQVEPDAK PAAYDPVMTD
LNGYIETAAE PEPEEDLFAP VAFAALPLGL DEPEDVRIEF APDASFYRNG HEPERIFTAL
GPDVSAVCDA DTVPLLSDFN VDTGYLVWSL EIKGKTESEV AEAFEYAKGL GRIDYLSDDA
PAPVGPVSEI AVEVPAPPST QAKPAKARPA SAQTLRIDPE RVDRLINTVG ELIINQAVIA
QKIEGDGTPV DPEVASALDD YRYLAREIQE AVMSIRAQPV KSLFQRMARV VREAGEATGK
AVSFETRGEA TEIDKTLIER LADPLTHMLR NAVDHGLESP EDRAATDKHA TGTVTLSAAH
RSGHVMIEVS DDGAGLDRAR ILKKAIANGL VAEDTNLSDT EIDNLLFAPG FSTADQVTNL
SGRGVGMDVV KTSITSIGGR VTITSEQGRG STFTILLPLT LAVLDGIVVS VADETMVVPI
ATIIETIRAS SDDVIELSPD NWVLKVRGAY VPIIDLAPLL GFRTERNAAG PFILVEAETG
AVYAFAVDEI WDQRQIVIKS LEGNYGAIPG ISAATILGDG QIALIVDPEA LIALAGPTAM
TSHKQKVGA
//
