ID A0A1G7KV29_9EURY Unreviewed; 665 AA.
AC A0A1G7KV29;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216218_10644 {ECO:0000313|EMBL:SDF41083.1};
OS Halorientalis regularis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF41083.1, ECO:0000313|Proteomes:UP000199076};
RN [1] {ECO:0000313|EMBL:SDF41083.1, ECO:0000313|Proteomes:UP000199076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF41083.1,
RC ECO:0000313|Proteomes:UP000199076};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FNBK01000006; SDF41083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7KV29; -.
DR STRING; 660518.SAMN05216218_10644; -.
DR OrthoDB; 293137at2157; -.
DR Proteomes; UP000199076; 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; IPR010808; CheA_P2-bd.
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 NCBIfam; NF041336; CheA_Halo; 1.
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 Pfam; PF07194; P2; 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:SDF41083.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:SDF41083.1}.
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 331..538
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 540..665
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 124..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 665 AA; 72019 MW; 69D350787C1D6FDA CRC64;
MDDQYLDAFI RESEEAITEL NNSLLALESD PEDEQAMESI FRTAHTLKGN FGAMGFEDAS
DLAHAIEDLL DEMREGNMEV TPEVMDMIFA GVDQIEVIVS EIEEHGESTT DTDEMVAEIR
GVLEDGPDAA DDGGDAGSDA AEEASDDTAE SEGDDADDGA DDGETDVTVD TSVFADASVD
ADEAYHVRVE IGDSNMLGVD GMLAVEAVAD TFGLLAAEPA RAKIEDGEYE GGFDLLVDAP
DTDVLRGSLS SVSKIDAFAV EHVDQFADDG EDGSDSGETA ASTDSSVDEI KSVRVDVDRL
DELHGQVEQL VTSRIKLRRA VADGDMDAAG ENLNELDKIS ANLQNTVMDM RLIPLKKVVG
KFPRLVRDLA RELDKEVDFR IEGEDIELDR TILTEISDPL MHILRNAVDH GIEPPEERER
KGKPREGTVE LRATRERDHV IIEVEDDGAG LDVADIREQA LEHGVRTEEE LDRMEEGEIY
DLAFHPGLST KDEVTDTSGR GVGMDVVHDT VTQLDGSVSV DSEPGEGTTV SLRLPVTMAI
VKVLFVQVGD EQYGVPIKNI DEISQMNGTK IINGEEVIEH NDDIYPIVDI AEAFDVPDAK
TNGDGMLVRI RESERQVALK CDAVTQQEEV VVKPLEGILS GTPGLSGTAV LGDGNIVHIL
DVVTL
//
