ID A0A368XU63_9BACI Unreviewed; 678 AA.
AC A0A368XU63;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=DFR57_10693 {ECO:0000313|EMBL:RCW70696.1};
OS Saliterribacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW70696.1, ECO:0000313|Proteomes:UP000252585};
RN [1] {ECO:0000313|EMBL:RCW70696.1, ECO:0000313|Proteomes:UP000252585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW70696.1,
RC ECO:0000313|Proteomes:UP000252585};
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 (JUL-2018) 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};
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:RCW70696.1}.
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DR EMBL; QPJJ01000006; RCW70696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368XU63; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000252585; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR035891; CheY-binding_CheA.
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 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; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Kinase {ECO:0000313|EMBL:RCW70696.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000252585};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 296..546
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 548..678
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 678 AA; 75288 MW; 3A4798C6A5DD04CD CRC64;
MEMNEYLEVF IEESKEHIQS LNQQLLILEN EPTNKATLSE IFRSAHTLKG MAATMGYQDL
ANLTHKMENV LDAARNDQIL INSEILDVVL ESVDHLETMV VDIAAGGDGK LNVEDSVGKL
QAIENGQEVQ SKLHTEKTKP AEQSNTSSRA SIELDQFETT VLQQSNENGF KNYLVEVKLN
ENCLLKAARV YMVFEVLEQT GEVIKSIPTV QELEEENFDL AFTVLIVSKE EAELIKQKIL
KVSEIESVSL TVFDVNNVNN TSQQEESVIQ ETPAPTTNTN DEAKDKDQTK TQNKAVATKT
IRVNIDRLDG LMNLFEELVI DRGRLEQISA NLKHPELQDT VERMSRISGD LQNIILNMRM
VPVEQVFNRF PRMVRQLSKD LGKKINLEIQ GAETELDRTV IDEIGDPLVH LIRNALDHGV
ENPEVRKQKG KIEEGQLLLN AYHSGNHVFI EITDDGAGIN QSKVIEKAIS NRVITEDEAA
MMTDSQVNQL IMASGFSTAD VISDVSGRGV GLDVVKNTIE SLGGSITIES EQDKGSKFSI
QLPLTLSIIS VLLVEVEREK YAVPLSSIIE TAIVNKSDIL YAHNKKVIDF RGKVVPLISL
KEVFEVPIED DEDELFSVVI VRKGDKMAGL IVDTFIGQQE IVLKSLGDYL GNVFAISGAT
ILGDGQVALI VDTNSLIR
//
