ID A0A0N7JHR3_9CAUL Unreviewed; 762 AA.
AC A0A0N7JHR3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AQ619_12625 {ECO:0000313|EMBL:ALL14114.1};
OS Caulobacter henricii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL14114.1, ECO:0000313|Proteomes:UP000056905};
RN [1] {ECO:0000313|EMBL:ALL14114.1, ECO:0000313|Proteomes:UP000056905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:ALL14114.1,
RC ECO:0000313|Proteomes:UP000056905};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-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};
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DR EMBL; CP013002; ALL14114.1; -; Genomic_DNA.
DR RefSeq; WP_062148106.1; NZ_CP013002.1.
DR AlphaFoldDB; A0A0N7JHR3; -.
DR STRING; 69395.AQ619_12625; -.
DR KEGG; chq:AQ619_12625; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000056905; Chromosome.
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; 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:SF1; 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; 2.
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; 2.
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:UP000056905}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 217..457
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 459..593
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 616..744
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 762 AA; 81312 MW; 03724F25C5FAE37F CRC64;
MDDLISDFLT EANESLEVID IELVRFEGHP GDRPALDKIF RLVHTLKGTC GFLGLGRLES
LAHAGETLLG RFRDGKLQVS GEAVTLVLRS IDRIKLVIDG LGATGTEPAG DDSDLIAALE
AMAMGAPGVE TPASAPEPEP EQQVEGYDPV LGRALRPGEV STADLDAAFA AAEGPVDSAP
PALTEPSAAI ADPRPVGTVE EDAAPIAATQ SIRVGVDVLE DMMTLVSELV LTRNQLLQIN
RGRTDDSFSP PLQRLSTITG ELQDSVMKTR MQPIGQAWKK LPRIIRDLAN ELDKKIDLVL
EGEATELDRQ VLEQIRDPLT HMVRNSADHG LEGPADRRTA GKAETGTIHL SAYHEGGSIV
IRLRDDGRGL DTARIREKAI EKGLLTRSDA EALSESQVHR LIFAPGFSTA AAITNVSGRG
VGMDVVRSNI EQIGGQIDLQ STFGSGCTVT IKIPLTLAII SALIVGASGE RFAVPQGAVL
ELIKIGDGAE HRTEVIEQVR MVRLREELVP LIDLGAELGL PQTSQPNFVM IMKVGSHRFG
VMVEEVIDTE EIVVKPLASV LRGISVFSGA TLLGDGSVVL IIEPNGLAQR AGEMPLAARR
AIDAAATNDD DAKIERKTML LVRVGSGALK AVELGQITRL EHVPVGELQH LGSRAALQYR
GKLMPVLCVD EDQRLKTEGV QPMLVVAGML YTMGLAVDRI VDVVETPVTI ELSPTKTGII
GTALINGRAT EIIDLDHFMI MALAEHARTG PASQAGQAQE AA
//
