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Database: UniProt
Entry: A0A6S6RA06_9FIRM
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ID   A0A6S6RA06_9FIRM        Unreviewed;       688 AA.
AC   A0A6S6RA06;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   08-OCT-2025, entry version 18.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cheA_3 {ECO:0000313|EMBL:BCJ95691.1};
GN   ORFNames=acsn021_32600 {ECO:0000313|EMBL:BCJ95691.1};
OS   Anaerocolumna cellulosilytica.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC   Lachnospiraceae; Anaerocolumna.
OX   NCBI_TaxID=433286 {ECO:0000313|EMBL:BCJ95691.1, ECO:0000313|Proteomes:UP000515561};
RN   [1] {ECO:0000313|EMBL:BCJ95691.1, ECO:0000313|Proteomes:UP000515561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN021 {ECO:0000313|EMBL:BCJ95691.1,
RC   ECO:0000313|Proteomes:UP000515561};
RA   Uek A., Ohtaki Y., Kaku N., Ueki K.;
RT   "Descriptions of Anaerotaenia torta gen. nov., sp. nov. and Anaerocolumna
RT   cellulosilytica gen. nov., sp. nov. isolated from a methanogenic reactor of
RT   cattle waste.";
RL   Int. J. Syst. Evol. Microbiol. 66:4306-4309(2016).
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; AP023367; BCJ95691.1; -; Genomic_DNA.
DR   RefSeq; WP_184093474.1; NZ_AP023367.1.
DR   AlphaFoldDB; A0A6S6RA06; -.
DR   KEGG; acel:acsn021_32600; -.
DR   Proteomes; UP000515561; Chromosome.
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; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric 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; IPR051315; Bact_Chemotaxis_CheA.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_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; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
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:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515561};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
SQ   SEQUENCE   688 AA;  77039 MW;  2C6A5A544A7FF72C CRC64;
     MSEQYSNDAL LESFIYETIQ LTEQLEQTVI ASEGKGGFLP EEINKVFRIM HTIKGSASMM
     RFQDISTLAH TIEDVFFILR ENSSTKSGDS LLCDLLLDSV DFIKSELEKI ENDMRADGSS
     SEIITALKKY LTSIKKNQRD AVTHKNTVNS ENHTTQFVQS STKKVSNFGQ DVKEEGNRFE
     VVIYFEENCG MEHVRAYGIV HALKDMVHSI TYLPENIGTD ASIEAIQANG FRIDLTSNLG
     YHALHHLLMS TVFLKELKLK QLNKSANEDN GSHISDVLNE TELTEEKNET EIRVKKKERT
     AYHSMISVSV AKLDKLMDLM GELVITEAAV LKKLDIEEMT LDIFHKSARQ LSKITSDLQD
     IVMAIRMLPL SVTFHKMNRV VRDMSKKLEK EVNLILVGED TEVDKNIIEH ISDPLMHLVR
     NALDHGIENP EERVSLGKTA IGTITLKAEN SGSEVLITIK DDGRGLNKDK ILTKAKKTGL
     LDKRESNLTD KEIYKLILLP GFSTKEKSTE FSGRGVGMDV VMKNLETIGG SLGVESRAGE
     GTTITLKIPL TLAVMEGMNL SVGDSNYIIP INVIKESFHP KEEDIIFHPN GNDMIRIRSK
     LYPILSLHKI FNVRANALNY SEGILIMVSR DEKSACLFAD HLTGQQQVVV RALPEYIQEA
     SERKILEGCT LLSDGRISLI LDIPGLIS
//
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