ID E9S9G7_RUMAL Unreviewed; 801 AA.
AC E9S9G7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CUS_6280 {ECO:0000313|EMBL:EGC04099.1};
OS Ruminococcus albus 8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC04099.1, ECO:0000313|Proteomes:UP000004259};
RN [1] {ECO:0000313|EMBL:EGC04099.1, ECO:0000313|Proteomes:UP000004259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:EGC04099.1,
RC ECO:0000313|Proteomes:UP000004259};
RA Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL Submitted (FEB-2011) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EGC04099.1}.
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DR EMBL; ADKM02000040; EGC04099.1; -; Genomic_DNA.
DR RefSeq; WP_002847596.1; NZ_JAJFOM010000001.1.
DR AlphaFoldDB; E9S9G7; -.
DR STRING; 246199.CUS_6280; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000004259; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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: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; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 4..114
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 418..654
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 656..795
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 363..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 801 AA; 87577 MW; D800BC9D302B073C CRC64;
MPKFDESMEG MLDTFLFETG ELLENLDEIL MRAEQAEDIS LIEESDIAEI FRTMHTIKGS
AAMMGLQNMS ALAHAMEDMF YIIREKTYVQ TDKSALFDLL YKSSDALKGE LEDLTDEDKP
LTDFSGLIND IHVLAAYFKG EAEKSGQEDN ALPADIFDEN EPPDMLTYRL TYSDSCEMPS
ARAIVLFRKL GAVAEVCRTI PPDMDDDGAD GKIKAAGLFI KLVTDDRAAV ERVLAAGMNV
ENFELFTPEM LKAQTSAAPA KQELVIPDGV FLPDDPDSLL TYRVMYSESC AMPSARAMVL
LRKLGAFAEV CRTVPADLDA DSADDEIAKN GLYIKLITDD TNAVERLLDS GINVESALPV
KKPAVPQKPA EPAPQEEKQE VGQAEKKPAE PKKTAAKAPK KEQSLLTVKL EKLDRLLDLV
SEIVITESAV TSSPDLRGLE TRLDRFNKSS RELKKLTDEL QDVVMSLRMV PVSTAFQKMN
RVVRDMNNTL KKNATLVFRG EDTEVDKSIV DMLGDPLMHI VRNAVDHGIE TPEERLAAGK
TNPPTVTLSA GYESNEVVIS CKDNGAGMDA AKILAKAKKN GMLTKPESEY TEKEIFNFVV
AAGFSTNEQV TQYSGRGVGM DVVKQNIEKV GGKLIVNSVL GKGSSFTIRI PLSLSILDVL
SVEVGASSIS IPASSIREAF SCKAESLITD PDGNEFVYLR DRCFPLIRLG EKLQIDTDIT
EPADGICMYC REGQYEAVLL ADRIVCDQQV VVKPFSPLLD GLHLKEAGLA GCSILGDGSM
TIILDMLSLL GGELGEEAQN G
//
