ID A0A089YIZ2_9PSED Unreviewed; 737 AA.
AC A0A089YIZ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-OCT-2025, entry version 51.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LT40_02550 {ECO:0000313|EMBL:AIS16338.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS16338.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS16338.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS16338.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
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; CP009533; AIS16338.1; -; Genomic_DNA.
DR RefSeq; WP_043186081.1; NZ_CP009533.1.
DR AlphaFoldDB; A0A089YIZ2; -.
DR STRING; 216142.LT40_02550; -.
DR KEGG; prh:LT40_02550; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_7_6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000029499; 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 FunFam; 2.30.30.40:FF:000048; Chemotaxis protein CheA, putative; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR FunFam; 1.20.120.160:FF:000008; Chemotaxis sensor histidine kinase 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; IPR051315; Bact_Chemotaxis_CheA.
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; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
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; 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:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 389..598
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 600..734
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 222..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..245
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 737 AA; 78777 MW; 887EEEEE2CD89BDD CRC64;
MSFGADEEIL QDFLVEAGEI LEQLSEQLVE LESRPDDADL LNAIFRGFHT VKGGAGFLQL
NELVECCHIA ENVFDILRKG ERRVDSELMD VVLEALDAVN GMFSEVRERA PVTPASPQLL
DALARLAEPA AVVAPPAAPV AVPVPVAAPA ATPSEDITDD EFEQLLDSLN AAKAQAATPI
AAAVARDGAA SDEITDDEFE SLLDQLHGKG QFAVDALAPT VTSEAAPGSG PASAAPVSST
PAAPGDEITD DEFEALLDQL HGKGTFTSEA VKVQPPAEVP APKSDQITDD EFESLLDQLH
GKGKFSDVAS VPDAQPVAAA AAVPVAAPRK TEAAPARAPV AEKPVASEAE TTVRVDTARL
DEIMNMVGEL VLVRNRLVRL GSNSSDEAMS KAVSNLDVVT ADLQTAVMKT RMQPIKKVFG
RFPRLVRDLA RQLKKEINLE LVGEETDLDK NLVEALADPL VHLVRNAVDH GIETPEERER
NGKARGGRVV LSAEQEGDHI LLSISDDGKG MDPAVLRAKA VEKGLMDRDA ADRLSESDCY
NLIFAPGFST KTEISDVSGR GVGMDVVKTK ISQLNGSINI FSAKDQGSKI VIKVPLTLAI
MPTLMVMLGN QAFAFPLVNV NEIFHLDLSR TNVVDGQEVV IVRDKALPLF YLKRWLVKSA
AHEEQGEGHV VILTVGTQRI GFVVDQLVGQ EEVVIKPLGK MLQGTPGMSG ATITGDGRIA
LILDVPSMLK RYATRRI
//
