ID A0A0R0DVF0_9GAMM Unreviewed; 565 AA.
AC A0A0R0DVF0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=ABB34_14060 {ECO:0000313|EMBL:KRG81443.1};
OS Stenotrophomonas daejeonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG81443.1, ECO:0000313|Proteomes:UP000050940};
RN [1] {ECO:0000313|EMBL:KRG81443.1, ECO:0000313|Proteomes:UP000050940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG81443.1,
RC ECO:0000313|Proteomes:UP000050940};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG81443.1}.
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DR EMBL; LDJP01000100; KRG81443.1; -; Genomic_DNA.
DR RefSeq; WP_057642000.1; NZ_LDJP01000100.1.
DR AlphaFoldDB; A0A0R0DVF0; -.
DR STRING; 659018.ABB34_14060; -.
DR PATRIC; fig|659018.3.peg.157; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000050940; Unassembled WGS sequence.
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 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000050940}.
FT DOMAIN 172..426
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 428..561
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRG81443.1"
SQ SEQUENCE 565 AA; 60451 MW; 3D9124E1C697601F CRC64;
AVLRALLREA EHGQPADPAA VAAVKARLEA VLSGTAAAPV VAKQEETAEP EGWQIGFVPA
PSLFMSGNDP LRIIRELETL GPLQVDARME RLPGFEQMDP LEAYIAWDLG LTGRIPRSKI
EDTFAWVVDD CELDIQPILA PPSLATSAPA PVQEAVAEAA PRPSAAGNAP ANAAHEAESS
IRVSVDKVDA LINLVGELVI TQAMLKQVSG GLDPSHAERL LAGLDLLERN TRDLQEAVIG
VRMLPVDAVF RRFPRLVRDL SSRLGKQVRL RTIGEGTELD KGLIEKIADP LVHLVRNSID
HGLEMPDVRK QAGKDETGTI TLAASHQGGH IVIEVSDDGR GLNRDKILAK AHERGLAIPD
NPSDAQVWDL IFQPGFSTAD AVTDLSGRGV GMDVVRRNIQ ALGGEVQLES HTGAGTRVLI
RLPLTLAILD GMTVSVAGET LILPLAYVLE ALQPKAEDIR TMAGEGRVLR VRGEYLPILS
LGNYYGYRTD SHADPLVVVV EGDGQKIALE VDELLGQQQV VVKNIENNYR RIGGVSGATI
LGDGRVALIV DVGGLVRSLR VPQAA
//
