ID M0E601_9EURY Unreviewed; 764 AA.
AC M0E601;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C471_05401 {ECO:0000313|EMBL:ELZ41789.1};
OS Halorubrum saccharovorum DSM 1137.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227484 {ECO:0000313|EMBL:ELZ41789.1, ECO:0000313|Proteomes:UP000011514};
RN [1] {ECO:0000313|EMBL:ELZ41789.1, ECO:0000313|Proteomes:UP000011514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1137 {ECO:0000313|EMBL:ELZ41789.1,
RC ECO:0000313|Proteomes:UP000011514};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ41789.1}.
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DR EMBL; AOJE01000015; ELZ41789.1; -; Genomic_DNA.
DR RefSeq; WP_004047035.1; NZ_AOJE01000015.1.
DR AlphaFoldDB; M0E601; -.
DR STRING; 1227484.C471_05401; -.
DR PATRIC; fig|1227484.4.peg.1109; -.
DR eggNOG; arCOG04403; Archaea.
DR OrthoDB; 293137at2157; -.
DR Proteomes; UP000011514; 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; 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 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ELZ41789.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:ELZ41789.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 391..610
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 612..764
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 101..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..411
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 110..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 764 AA; 80199 MW; 7130902C0E731CA0 CRC64;
MDSHRAAFVA EAEDGITDLN NALLALEADP EDAEAMDDVF RVAHTLKGNA AAMGYEDVSD
FGHALEDLLD AVRQGDREVT PELMDLLFEG VDTVEAMVSE IADTGDVSTD PSDLESRLRE
MEEHGTVGGE DAGSDDGSDA GEVDDTDADD SDEGGEADEG PAEESDENTE DDADAVSVPE
LPDAAAALDG PVVYADVTIG EAAMAGVDAA LVLQALDDQF GEHVTVPNPE ALEDGEYDER
FDAFVADADP AVVAEGIGAL TQVESIATAL VGDSDEGGEA DAVDSGGDAE LGAEADAESG
VGADAESGVG ADAESGAEAD DDADAEDGAE ADDDADAEDG ADTEDDADDG SSDTKSDSKS
GDEIKSIRVD VDQVDELYGL VEQLVTSRIK LRRELEELNA QSDALDELDK LASSLQDTAM
DMRLIPFSQV SDSFPRLVRD ISRDLDKRID FEIEGDDVEL DRTILTEMRD PLVHVLRNAV
DHGIETPEER EAAGKDPTGH VRLTAERERD HVIIEVADDG GGLDPDQLRE KAVDEGVKSR
EAVEAMEDDE VYDLVFHPGF STAEEVTDVS GRGVGMDVVR TTARDLDGSV SVESEPGEGT
TVRFRLPVTV AIVKVMFVDV GGTEYGIPIK SIAEVARADD IEEVHGDEIV RHEDDLYPVI
RLNERLANGG AAAVGSGAGD ATEVDTAGGE SASATTDGGV TDEGMLVRIR EETRQVALHC
DAVLDQEEVV VKPLDGPLSG TPGLSGTAVL GDGDVVAVLD VVSL
//
