ID A0A1I6XWM9_9FIRM Unreviewed; 713 AA.
AC A0A1I6XWM9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02910301_0999 {ECO:0000313|EMBL:SFT42616.1};
OS Lachnospiraceae bacterium XBD2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520820 {ECO:0000313|EMBL:SFT42616.1, ECO:0000313|Proteomes:UP000199425};
RN [1] {ECO:0000313|EMBL:SFT42616.1, ECO:0000313|Proteomes:UP000199425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBD2001 {ECO:0000313|EMBL:SFT42616.1,
RC ECO:0000313|Proteomes:UP000199425};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FPAN01000003; SFT42616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6XWM9; -.
DR STRING; 1520820.SAMN02910301_0999; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199425; 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: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; 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 Kinase {ECO:0000313|EMBL:SFT42616.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000199425};
KW Transferase {ECO:0000313|EMBL:SFT42616.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 337..582
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 584..713
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 129..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 713 AA; 77248 MW; 69598C755BE6DB00 CRC64;
MDVSQYLDIF IDETNEHIQS LSDNIMALEQ EPENKDTINE IFRAAHSLKG MAGTMGFKRM
QHLTHDMENV FSEVRNDTIK VNSNLIDILF QCLDAIEGYL DNVKNTSDEG TEDNEVLIKQ
LNDYLNGASG DSAAPAADEA TAEAPAEGAP AAEAAEGEEY KTLKLDDSDK GKLKSAQESG
LNLYGFTLHI HPECLLKAAR AFLVFKALED YGEILIYNPS AQEIEDEKFE FTFSCIVGCS
GDDLNAMKEA VSAVSEIESV ECGKVTYEMY EQASEAAPAA EAPAPEAAPA AEAAPAAPAP
AASSAPAPAA KKNAPAANNK KAANKPVTAR TVRVDIEKLD DLMNQVSELI IAKNSIVSIS
SSDSKAGDMD QTFREQVEYL ERITTSLHES VMKVRMVPIE STVNKFPRMI RDLSRKLNKP
MELVMTGEET ELDRTVVDQI GDPLQHLLRN SADHGIESPE VRKAAGKPEQ GTIFLNAFQE
GNNVIIQVGD DGAGINTEAV LNKAIERGLV TAEEAENLSQ KEIIDFLFNP GFSMAKQITD
ISGRGVGLDV VKSNIEALGG DVEVKSELGQ GSTFTVRLPL TLAIIQALMV EVRDEKYAIA
LGSIMTIEDI PTSDIKYVQA KEVIHLRGLV IPLIRLGELL DFEPMEEEPD TLIVVIVKKG
DNYAGLVVDN LIGQQEIVIK SLGKVIENNK IISGATILGD GEVAMILDAN ALI
//
