ID A0A1M7T5K2_9RHOB Unreviewed; 672 AA.
AC A0A1M7T5K2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216200_104192 {ECO:0000313|EMBL:SHN65968.1};
OS Oceanicella actignis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Oceanicella.
OX NCBI_TaxID=1189325 {ECO:0000313|EMBL:SHN65968.1, ECO:0000313|Proteomes:UP000184066};
RN [1] {ECO:0000313|EMBL:SHN65968.1, ECO:0000313|Proteomes:UP000184066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10808 {ECO:0000313|EMBL:SHN65968.1,
RC ECO:0000313|Proteomes:UP000184066};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; FRDL01000004; SHN65968.1; -; Genomic_DNA.
DR RefSeq; WP_072747146.1; NZ_FRDL01000004.1.
DR AlphaFoldDB; A0A1M7T5K2; -.
DR STRING; 1189325.SAMN04488119_104192; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000184066; 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:SHN65968.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000184066};
KW Transferase {ECO:0000313|EMBL:SHN65968.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 275..526
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 528..662
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 130..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 672 AA; 72363 MW; 2365D2D4F3838D2A CRC64;
MEEDEDYEAL FFAECADLLG DLQEQLDRIA DGDEDPETIN AAFRAVHSVK GGAAAFGFTD
LIGFAHIFET VMDGIRSGRL EATPDLAMIL VRAGDAMAHL VELASQGGGE PEAIVPRVKA
ELEEVAAQLG AEAAPKPQPE PEPAAESASQ MGEAASREIR IRFAPGPDFF ARGHDPLRIF
RAARELGLMS AEVEGEAPPL SDLSFEACPF VWTLTFDTDR PDAEIDAFFD VCADAASIER
LDGETPTDPP APTEPAARKQ PTPQPAASAK KSGGGVARSL RVDLARVDKL VNLVGEIVIT
QAVLAQKLAE IDGAMTLEAG HSLEALNRQT RELQESVMTI RAQPVKSVFS RMPRIVRDLS
ETLGKRARLV ISGENTEVDT TVIEELTEPL THMLRNSMDH GLESAEERRA AGKPEEGVIH
LSAEHRGERV IIQITDDGRG IDRDRVLAKA MERGLVGPGE SLTPEEIDAL IFHPGFSTSE
KVSSVSGRGV GMDVVKKKIQ SLGGRCTVRS EPGKGTEFTI TLPLTLAVLD GMTIRVGSER
FVLPLSSVIE AVRLEDCDVR EMHDGSRMIG VRGAYLRLIS LRKTLGLPPA DAPETMAVVA
DTETDGHVAL LVDELIGQRH VVLKSLETNF KRIDGVSGAT ILGDGRVALI LDVPSLASLG
LPRRTMQQET VH
//
