ID A0A173L325_9SPHN Unreviewed; 655 AA.
AC A0A173L325;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EP837_03601 {ECO:0000313|EMBL:ANI79985.1};
OS Sphingobium sp. EP60837.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI79985.1, ECO:0000313|Proteomes:UP000078304};
RN [1] {ECO:0000313|EMBL:ANI79985.1, ECO:0000313|Proteomes:UP000078304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EP60837 {ECO:0000313|EMBL:ANI79985.1,
RC ECO:0000313|Proteomes:UP000078304};
RA Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT "Complete genome sequence of a organophosphorus pesticides.";
RL Submitted (JUN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP015987; ANI79985.1; -; Genomic_DNA.
DR RefSeq; WP_066531381.1; NZ_CP015987.1.
DR AlphaFoldDB; A0A173L325; -.
DR STRING; 1855519.EP837_03601; -.
DR KEGG; sphb:EP837_03601; -.
DR PATRIC; fig|1855519.3.peg.3717; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000078304; Chromosome 2.
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; 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; 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 PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ANI79985.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000078304};
KW Transferase {ECO:0000313|EMBL:ANI79985.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 261..524
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 526..655
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 655 AA; 69591 MW; F78369CF9AC1E47A CRC64;
MDELLEQFIL EGRDLVADAH SVLVALSRDP QNRTALDSLF RSVHTLKGSV ALFEMAPAEE
MLHAAETRLE AARRRDALLD ERALDAVLAV IDQTDRWIDA MQMTGSLSEG AEAQADRLIA
MLLADDGAGG TEADGRPHPM AALVTQEADW LVALRSRPEF SPVGLQQAQT AFRYTPDADC
FFRGEDPLAI SAAVPDLLAL AVLPAAGEWP AIASCEPFRC ISVIEGISGG DEAAVRAAFR
LMPDQAAVAP LGSVLEAPLP DVGPQPKDPS SMLRVEASRL DRLASQIGEL TVAIRTLRPI
ADRLRALDPL LAAELSAADD EIGRVAAEVQ RSVARVRQVS LEPVLRRLPR LAREAAANLG
KPVRFILEGE TARVDKEVAD QLFEPLLHIV RNAVDHGIEP ASERTAHGKP PEGKIHLSVR
PEGNGIKIMI ADDGRGIDAR ALRETAIAKR LMNSDAAAAL SDAEALQLIF LPGFSTAERA
TSLSGRGVGM DAVKAAVEKL AGTIAVESEV GQGTHIALRL PANALTTPLV VVGAGGQQLG
IRLDQIVETA RISASAIHPL GQKAQACVLR EETVPVLDLA SLLGFEPASG GIARLLITDI
GPCRTALRVD SLDERFDGVV RRADGLLTAL PAIAGTAMMT DGRILLVLDL PELMA
//
