ID A0A370X0T5_9GAMM Unreviewed; 660 AA.
AC A0A370X0T5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DWU99_15485 {ECO:0000313|EMBL:RDS81825.1};
OS Dyella psychrodurans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1927960 {ECO:0000313|EMBL:RDS81825.1, ECO:0000313|Proteomes:UP000255334};
RN [1] {ECO:0000313|EMBL:RDS81825.1, ECO:0000313|Proteomes:UP000255334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4MSK11 {ECO:0000313|EMBL:RDS81825.1,
RC ECO:0000313|Proteomes:UP000255334};
RA Gao Z., Qiu L.;
RT "Dyella monticola sp. nov. and Dyella psychrodurans sp. nov. isolated from
RT monsoon evergreen broad-leaved forest soil of Dinghu Mountain, China.";
RL Submitted (JUL-2018) 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:RDS81825.1}.
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DR EMBL; QRBF01000006; RDS81825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370X0T5; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000255334; 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 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: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 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 308..519
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 521..656
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 660 AA; 70232 MW; 71A8428F7B4700AA CRC64;
MSTISVTQFH KVFFEESLEG LDAMETALLA LDEGGDAELV HSIFRAAHSI KGGAATFGFP
EMAAFTHEAE SLLDQVREGR RAIDKPIIEL MLRTVDCLRG MFERAQGGQP LADASSEELK
RQLAAAVGRE VPAPTAKVAA KPAASNGWSI KFRPHAGMLA GGNDPLRLLR ELAALGQLVV
EAQLDRVPTL DALDPSECHL GWHLTLTGAA TREAIASVFE WVEDECDLSI EPLVAAAPPP
APAVETDAAP AGAGAAAGTT RSAAASSNDA GSVRVGIDKI DSLIDLVGEL VITQAMLDQF
REDFDPSRLS MLQEGLAQLA RHTRSLQESV MGIRMLPIGS VFNRFPRLVR DLSQKLGKQV
KLELVGEHTE LDKTVLEKIG DPLVHLVRNA IDHGLEIPEK RRAAGKGDVG TLRLEASHRG
GSIVVEIVDD GAGLNREAII NKALQKGLIK SAEGISDEEV GELIFQPGFS TAAVTTDLSG
RGVGMDVVRR NVVDLGGNVA IKSRPGNGTT FTITLPLTLA IIDGLSAGVG DECYIVPLVS
IVESIQLPAE AVRSVTGGGE LFRFRDEYLP IVRLHQQFGC ATARQKIEEG LVIVVEADGN
RVGLFVDELI GQQQAVVKSL EANYRRVDGI SGATILADGS VALIVDVAGI IRLQARRKAA
//
