ID A0A1G9XXD9_9BACI Unreviewed; 672 AA.
AC A0A1G9XXD9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216498_1150 {ECO:0000313|EMBL:SDN01448.1};
OS Tenuibacillus multivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tenuibacillus.
OX NCBI_TaxID=237069 {ECO:0000313|EMBL:SDN01448.1, ECO:0000313|Proteomes:UP000199334};
RN [1] {ECO:0000313|EMBL:SDN01448.1, ECO:0000313|Proteomes:UP000199334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3442 {ECO:0000313|EMBL:SDN01448.1,
RC ECO:0000313|Proteomes:UP000199334};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNIG01000002; SDN01448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9XXD9; -.
DR STRING; 237069.SAMN05216498_1150; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199334; 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:SDN01448.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000199334};
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 332..539
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 541..672
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 252..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 672 AA; 74798 MW; 6D3AA6C80A132FC8 CRC64;
MDTNQYLEVF IDESTENLQV VNDRLLDLEK NADDLSIVND IFRAAHTLKG MSATMGFEDL
ADLTHKLENV LDAIRNEQIN VSTSILDVLF DSVEALEDMI SDISNGGDGK KDVQAIVGQL
KAIESGEAVG ENESPKSETA TQLSSDISLD EFEQTVLEEA LSQGQHVYHI SVSLAEDCLL
KAARVYMVFE VLEQSGEVIK SIPTVEQLED EQFDETFDII VVSEQDDEAI KAKIYKVSEV
KDVQIKAFDS SRIRSEEEGT TEEEVSATTE AKPEKESEET DSPKRQKAVS NKTIRVNIER
LDTLMNLFEE MIIDRGRLEQ ISREIEHQDF RETVERMTRI SSDLQNVILT MRMVPIEQVF
NRFPRMVRNL ARDLGKKIDF QIEGAETELD RTVIDEIGDP LVHLIRNAVD HGIETPEKRA
ASGKSETGRL ILKAYHSGNH VFVEIKDDGG GINQDKVLQK ALKNDIITNE QASNLNDRQI
FELIMASGFS TADQISDISG RGVGLDVVKN TIESLGGTIE IDSEYGEGTT FSIKLPLTLS
IISVLLVVLK DETFAVPLSS IIETAVIHKK EIYKARGREV IDFRGNIVPL VHLKEVFAVE
QDQDNADDYY SVVIVRKGDQ MAGLVVDSFI GQKEIVLKNL GQYLKDVFAI SGATILGDGE
VALIVDTNAL IK
//
