ID Q89XC1_BRADU Unreviewed; 949 AA.
AC Q89XC1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=bll0393 {ECO:0000313|EMBL:BAC45658.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC45658.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC45658.1; -; Genomic_DNA.
DR RefSeq; NP_767033.1; NC_004463.1.
DR RefSeq; WP_011083225.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89XC1; -.
DR STRING; 224911.AAV28_41210; -.
DR EnsemblBacteria; BAC45658; BAC45658; BAC45658.
DR GeneID; 64020249; -.
DR KEGG; bja:bll0393; -.
DR PATRIC; fig|224911.44.peg.8919; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_5_1_5; -.
DR InParanoid; Q89XC1; -.
DR OrthoDB; 9803176at2; -.
DR PhylomeDB; Q89XC1; -.
DR Proteomes; UP000002526; 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; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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 Pfam; PF00072; Response_reg; 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 SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 2.
DR SUPFAM; SSF52172; CheY-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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT DOMAIN 1..100
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 233..514
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 516..654
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 820..936
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 234..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 869
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 949 AA; 101293 MW; 0D144108053B3443 CRC64;
MDDLLREFLT ETSESLDTVD NQLVKFEQEP NNAKILDNIF RLVHTIKGTC GFLGLPRLEA
LAHAGETLMG KFRDGMPVTG QAVTVILSSI DRIKEILAGL EATEAEPEGT DRDLIDKLEA
MVEQGMAAMS ASASPIASGS AQPMPAAGSA AAVADAPPLV PEAPAAAAPA KDMTTGSLID
QTLERPLRPG EVSLDELERA FRETAIEAPI PAPIVKAEVK AEPAPAPAPV AKEAAKEAAK
PAAKEKAAPK KSMADEGASE GDRIANQSIR VNVDTLEHLM TMVSELVLTR NQLLEISRRN
EDTEFKVPLQ RLSNVTAELQ EGVMKTRMQP IGNAWQKLPR IVRDLSSELG KQIELEMHGA
DTELDRQVLD LIKDPLTHMV RNSADHGLET PAERLAAGKG EQGTIRLSAY HEGGHIIICI
ADNGRGLNTE RIKAKAISSG LVTEAELEKM SEAQIHKFIF APGFSTAAAI TSVSGRGVGM
DVVRTNIDQI GGTIDIKSVA GEGSSVTIKI PLTLAIVSAL IVEAAGDRFA IPQLSVVELV
RARANSEHRI ERIKDTAVLR LRNKLLPLIH LKKLLKIDDG AASDPENGFI VVTQVGSQTF
GIVVDGVFHT EEIVVKPMST KLRHIDMFSG NTILGDGAVI MIIDPNGIAK ALGAAGSSAH
DMGDENGAHH IGSGEQTTSL LVFRAGSSQP KAVPLGLVTR LEELPADKIE FSNGRYMVQY
REQLMPLVAM ESVTVASQGA QPILVFADDG RSMGLVVDEI IDIVEERLNI EVGGSSQGIL
GSAVIKGQAT EVIDVGHFLP MAFADWFTRK EMKPSMHSQS VLLVDDSAFF RNMLAPVLKA
AGYRVRTAPT AQEGLAALRA QSFDVVLTDI EMPDMNGFEF AEVIRSDNNL GAMPIIGLSA
LVSPAAIERG RQAGFHDYVA KFDRPGLIAA LKEQTAGAAG ASELSRAAA
//
