ID A0A3N1NUU0_9GAMM Unreviewed; 767 AA.
AC A0A3N1NUU0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EDC38_0556 {ECO:0000313|EMBL:ROQ19965.1};
OS Marinimicrobium koreense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Marinimicrobium.
OX NCBI_TaxID=306545 {ECO:0000313|EMBL:ROQ19965.1, ECO:0000313|Proteomes:UP000273643};
RN [1] {ECO:0000313|EMBL:ROQ19965.1, ECO:0000313|Proteomes:UP000273643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16974 {ECO:0000313|EMBL:ROQ19965.1,
RC ECO:0000313|Proteomes:UP000273643};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-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:ROQ19965.1}.
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DR EMBL; RJUK01000001; ROQ19965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1NUU0; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000273643; 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: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:0000313|EMBL:ROQ19965.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000273643};
KW Transferase {ECO:0000313|EMBL:ROQ19965.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 416..629
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 631..765
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 129..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 767 AA; 81611 MW; 7637B18AD5B83EBF CRC64;
MGFGDDEEIL QDFLVEAGEI LEKLSEQLVE LEQRPDDADL LNAIFRGFHT VKGGAGFLQL
DPMVECCHVT ENLFDVLRNG QRQVTSELMD VVLQSLDTIN QQFAEVSQRE DMSSADPQLI
DTLQRLVNGE PIDGGADTTS ESDQSHGSGE PVGNDTPKAQ GDITDDEFEQ LLDAIADEPG
AAPAKSGSDS KPSPEQGDVI QEDEFEALLD ELHGKGKGPG ASQPAKPSSE APASESDEID
DDEFEALLDQ LHGKGKGPGT GTPAKSAAPE PSAPAQAPAE SGKSASGNSS NNDLISDDEF
ESLLDELHGK GQGPTRKQPD ASGKPDTSAA AKPDSAPSAP KAASPAPAAP AGGGAGDGKK
PPASRPAGKP ADRDGGPAPA ETTVRVDTQR LDEIMNMVGE LVLVRNRLVR LGDDIENESL
AKAVSNLDVV TADLQTSVMK TRMQPIKKVF GRFPRVVRDL ARNLKKEVNL ELVGEDTDLD
KNLVEALSDP LVHLVRNSVD HGIELPDLRE ANGKPRTGKV VLAAEQEGDH ILLSITDDGA
GMDPDKLRDI AVEKGVMDRD SANRLSDTEA FNLIFAPGFS TKKEISDVSG RGVGMDVVKT
KITQLNGTIE IQSTKGEGTR LNIKVPLTLA IMPTLMVMLA EQAFALPLAS VQEIFHMDMS
KTHTVDGQEC VTIRDRAIPV FYLKDWLITG PRKAREREAH VVIVAIGTRM VGFVVDQLIG
QEEVVIKPLG KMLQGTPGMA GATITGDGTM ALILDIPGLL KRYAGGV
//
