ID A0A099TEP9_9RHOB Unreviewed; 726 AA.
AC A0A099TEP9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PM04_01120 {ECO:0000313|EMBL:KGL02619.1};
OS Thalassobacter sp. 16PALIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobacter.
OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL02619.1, ECO:0000313|Proteomes:UP000029829};
RN [1] {ECO:0000313|EMBL:KGL02619.1, ECO:0000313|Proteomes:UP000029829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL02619.1,
RC ECO:0000313|Proteomes:UP000029829};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09.";
RL Submitted (MAR-2014) 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:KGL02619.1}.
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DR EMBL; JHAK01000001; KGL02619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099TEP9; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000029829; 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:UP000029829}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 326..577
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 579..715
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 282..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 726 AA; 77431 MW; 74930A112448C92E CRC64;
MDPMAEIKAS FFVECSELLE SLEEGLLQVQ GGDTDPETVN AVFRAVHSIK GGAGAFGLDD
LVHFAHRFET VLDEVRSDRL AIDADAVLLF LKSADSLSDL VAAARDETPV DEAKNAVVIA
ELETLMPGGS DADEATTDAD QDLDFAPMTL SIDLPAIDAQ VDADIDEVAD EAAGTTPVWT
IRFATDKGLN QSGNEPLFLM RALAELGPVI AICDASDLPP LKVLDPSQTN LHWDLTLSAD
TSQTDIEEVF EFAQGLCTLA ITKKTSDQST PDTADLEALP VLPDLPTLPD LPAPSVDDQA
PAQPAAENTA PEAPKPPAPT PTKAAPVAAT VRVDLERIDR LVNLVGELVI NQAMLSQSLS
AQNLTSNTTI STGLDEFQQL TRDIQDSVMA IRAQPVKPLF QRMSRIVREA AHDTHKKVRL
VLEGEATEID KTVIERLADP LTHMIRNAVD HGLETPEKRE QSGKEPEGTI HLRATHRSGR
VVIEIQDNGA GINRERVLSI AQSKGLVPTD AVLSDAEIDN LLFMPGFSTA KEISNLSGRG
VGMDVVKRAI QSLGGRISIQ STPGHGSTFS ISLPLTLAVL DGMVIEVSEQ TMVVPLSSIV
ETLTLADAEI QTLDQGTQVV HIRGKFVPLL DLAVEFGYRA PNVIPEDAVV LFISAEDGEP
YALVVDTIHE QRQVVIKGLA DSYGYVPGVA AATILGDGKI ALILDPVDLI ARAGSPDTPT
ALSMAG
//
