ID A0A1T4X9I0_9CLOT Unreviewed; 655 AA.
AC A0A1T4X9I0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05443428_10741 {ECO:0000313|EMBL:SKA86117.1};
OS Caloramator quimbayensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=1147123 {ECO:0000313|EMBL:SKA86117.1, ECO:0000313|Proteomes:UP000190105};
RN [1] {ECO:0000313|EMBL:SKA86117.1, ECO:0000313|Proteomes:UP000190105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 833 {ECO:0000313|EMBL:SKA86117.1,
RC ECO:0000313|Proteomes:UP000190105};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUYH01000007; SKA86117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4X9I0; -.
DR STRING; 1147123.SAMN05443428_10741; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000190105; 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:SKA86117.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:SKA86117.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 321..526
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 528..655
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 253..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
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 655 AA; 73772 MW; BFB04FC1F1C116D9 CRC64;
MDMSQYLDMF LEESAENLQY LNDGILSLEK NPDEKETINS IFRAAHTLKG MAGSMGFTDI
AELTHKMENV LDKFRKDELS VTSDVVSILF KCVDALENMI NSIQEGNDDK FETKEIIEML
ENIQSSKAAI NINTADEKNE IEYDLNDYDK EIIKQAKDKN YKIYRVDTTL YKDCVLKSAR
AFLVYKTLEE AGELIKAVPS IEDLEQEKFD RSFSIMLITE KKIEEIRNLI MGISEIEKVE
VFEIKNEAEA EAAPAKEAIA DTSSLENGKN EKEEDKTNKK SHQSIRVDIE RLDKFMNLVG
ELVMHRTRLE QISIDLKKTE LHETLEQVGR ITLDLQDLVM KVRMLPIERV FNRFPRTVRD
LSKELNKDIE LIIEGEDTEL DRTVIDEIGE PIMHLIRNAA DHGIEPVEER IKNGKSPKGT
IKLMAYQEGN KAVIRLEDDG KGLDIEKIKN KAKKIGIETD GMSAADIKNL IFMQGFSTSD
KITDVSGRGV GMDVVKTKIS SLGGTVDVIS EAGKGTAFVI RLPLTLSIIQ ALLVKVGQET
FAISLGFIEK VINMNIDDIK KTNKKDVIVY RDNIIPIVRL SDKLNVEDEN SKQKYVVIVK
VGEKTAGLLV DSLLGQQEIV IKPMGRMLQN LKEYVGATIL GDGLVTLILN VAAFV
//