ID A0A1H5VZ77_9RHOO Unreviewed; 716 AA.
AC A0A1H5VZ77;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-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=SAMN05216242_11014 {ECO:0000313|EMBL:SEF92565.1}, Tchl_0425
GN {ECO:0000313|EMBL:APR03297.1};
OS Thauera chlorobenzoica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=96773 {ECO:0000313|EMBL:APR03297.1, ECO:0000313|Proteomes:UP000185739};
RN [1] {ECO:0000313|EMBL:SEF92565.1, ECO:0000313|Proteomes:UP000236741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB-1 {ECO:0000313|EMBL:SEF92565.1,
RC ECO:0000313|Proteomes:UP000236741};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APR03297.1, ECO:0000313|Proteomes:UP000185739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB1 {ECO:0000313|EMBL:APR03297.1,
RC ECO:0000313|Proteomes:UP000185739};
RA Goris T., Mergelsberg M., Boll M.;
RT "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT degrading haloaromatics anaerobically to CO2 and halides.";
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP018839; APR03297.1; -; Genomic_DNA.
DR EMBL; FNVJ01000010; SEF92565.1; -; Genomic_DNA.
DR RefSeq; WP_075146935.1; NZ_FNVJ01000010.1.
DR AlphaFoldDB; A0A1H5VZ77; -.
DR STRING; 96773.Tchl_0425; -.
DR KEGG; tcl:Tchl_0425; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000185739; Chromosome.
DR Proteomes; UP000236741; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.70.400; CheY-binding domain of CheA; 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; IPR015162; CheY-binding.
DR InterPro; IPR035891; CheY-binding_CheA.
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; PF09078; CheY-binding; 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; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:APR03297.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:APR03297.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 304..554
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 556..691
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
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 716 AA; 75848 MW; 941FB2B3D03059E4 CRC64;
MDISEFLDSF FEEAVELLAD MEGHLLELDC SAPDPEQLNA IFRAAHSIKG GAGAFGFQRL
QETTHIFENL LDHARRGELT LRKDIVDLFL ETKDMLQDQL EAYRSGGEPD QAAFERICRV
LQQLALEEIG KGAGEPGSAP AQAVEAPPPP PPPPVVAEPV ATEPAMAGGA GGHGERRLQV
SLLGVPAKDR ALLLEELAHL GTLCAQQGGD ARYDIELLTA VDADDIEAVL YFIIEAEQLQ
ITPLAAAPAA SGAAPAPAVT AAPAPAAAVV PAPAPVPPAA PEAAKPAAGK AAPAKAAAAA
KGGSESSSIR VPVEKVDQII NLVGELIITQ SMLEQTASGL DDVTHTALLN DMGVLQRNAR
DLQEAVMSIR MVPMDYVFSR YPRLVRDLAG KLDKDIELVT EGESTELDRS LTERIIDPLT
HLVRNSLDHG IEPPAVREAA GKPRCGRLTL SAQHQGGNIL IEVSDDGAGL NRDKLLAKAR
EKGLAVADTM SDDEVWQLIF APGFSTAEQV SDVSGRGVGM DVVKRNIQSM GGRVEIFSRL
GEGTTTRIVL PLTLAILEGM SIRVGEEVFV LPLSAVLESL QPRAEELHSM GGDDVVLKVR
GEYLSVIPVH EALAVDGACT DPVGCIAVIV QAEGRRHALL VDELIGQQQV VVKNLETNYR
KVPGVSAATI LGDGRVALIL DIGGLHRLSR AAKTSAATPG RAQEVRKTST KEVETL
//
