ID A0A2T4IC02_9RHOO Unreviewed; 673 AA.
AC A0A2T4IC02;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-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=C8261_14830 {ECO:0000313|EMBL:PTD95293.1};
OS Pseudothauera lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Pseudothauera.
OX NCBI_TaxID=2136175 {ECO:0000313|EMBL:PTD95293.1, ECO:0000313|Proteomes:UP000241193};
RN [1] {ECO:0000313|EMBL:PTD95293.1, ECO:0000313|Proteomes:UP000241193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D20 {ECO:0000313|EMBL:PTD95293.1,
RC ECO:0000313|Proteomes:UP000241193};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PTD95293.1, ECO:0000313|Proteomes:UP000241193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D20 {ECO:0000313|EMBL:PTD95293.1,
RC ECO:0000313|Proteomes:UP000241193};
RA Liang Q.-Y.;
RT "Thauera lacus sp. nov., isolated from an saline lake in Inner Mongolia,
RT China.";
RL Submitted (APR-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:PTD95293.1}.
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DR EMBL; PZKC01000014; PTD95293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4IC02; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000241193; 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 Reference proteome {ECO:0000313|Proteomes:UP000241193}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 280..530
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 532..667
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 258..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 673 AA; 71084 MW; 502788C35A6B135D CRC64;
MSFDMSQFYQ VFFDESEEHL AAIEAILLRI DPAAPPAEGI AEIFRAAHSI KGSAATFGFD
DMATLTHAME NLLDRVRKGE LALQRGMVEA VLAACDVLRA QLDAHRGSAG AADPQAAAVA
LARLQACGEV PAAPPPQGGH GDGLELNFVL SRVVAGSEVL IDSLFDALGE LGEVRTLSRP
PADAADGVWT LALRGCAAEE RVRAALDLFV EPGTLEIAAL AAPSAAAAMQ PLPGEEIAAD
GSYGFFLPAP QPAALDDVPP VSPPASPPVA AEEGGRERTG TGHSIRVGVD KVDQMINLVG
ELVITRSILQ EAANVVDPAL AERLLAGLGL LERNTRELQE SVMAIRMVPI SRVFSRFPRL
VRELADSLGK EVELVLAGEH TELDKSVVER VADPLTHLVR NALDHGLEGP QERLAAGKAA
RGRLSLSARH EGGQIVIEVA DDGRGLDRQR VLARARASAL PVDEGMSDAE LWQLLFLPGF
STAESVSALS GRGVGMDVVR HNVDALGGSI ELDSVDGVGT RVVVRLPLTL AIMDGMTVAV
GRETYVLPLA QIVESLQVDA EAVHRIGGVA RMIRVRGEYL PVVALGERFA VPGAERDWLR
AIMVLVEAGG RRAALMVDAL LGQQQVVIKS LETHYRRVHG FSAATILGNG EVALIVDVGA
LVDASRVQAE LAA
//
