ID A0A1X1Q509_9FIRM Unreviewed; 722 AA.
AC A0A1X1Q509;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D081_1418 {ECO:0000313|EMBL:ORT99837.1};
OS Anaerovibrio sp. JC8.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORT99837.1, ECO:0000313|Proteomes:UP000192538};
RN [1] {ECO:0000313|EMBL:ORT99837.1, ECO:0000313|Proteomes:UP000192538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC8 {ECO:0000313|EMBL:ORT99837.1,
RC ECO:0000313|Proteomes:UP000192538};
RA Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT effect of hydrogen.";
RL Submitted (OCT-2012) 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 -!- 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:ORT99837.1}.
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DR EMBL; ANBM01000006; ORT99837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1Q509; -.
DR STRING; 1240085.D081_1418; -.
DR Proteomes; UP000192538; 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; 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:ORT99837.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:ORT99837.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 378..582
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 584..722
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
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 722 AA; 79509 MW; 07194FAA19CA6244 CRC64;
MAEPMVEVFI FETRQFLEQL EQIALGSEEQ GGFSEEDVNE IFRAMHTIKG SAAMMMFDQV
STLAHSVEDI FFYIRELKPA KVDATAITDI VLNAVDFMRI EMDKLDAGGT PDMSSEELRA
YTKDFLRNMK LDNGHDPDID LRKAKNAKKS SEATGEGASA PAPEPEPEKK QYYIGAAKPA
APAPAAEGTS GTQHVFEATV FFQQGCEMEE VRAFGVVNNM KEKVKELHYL PEKILEDESA
TDTIRNMGFR LFFTTDLNYD EVKAELDQTI FLDRLELKEV GSVAELEYWP SQETIAITAL
ENSEPIKPDM PPVQRDLSGP VKKPAPAKGG DGAQMITVRV DKLDKLMDLV GEMVIAEAMV
TQNPDLKGME LDNFAKAARQ LHKINGELQD SVMALRMVPL EGTFKKMNRI VRDMTKKLGK
KARLVLVGES TEVDKNINEH ISDPLMHIVR NSVDHGIEMP EVRVEAGKEE MGTVILSAEN
AGGEVVIKIK DDGGGLNKEK ILERARKNGI LTKPESELTD REIYSFIFAP GFSTKEAVTE
FSGRGVGMDV VVSNIKSLGG KVIVDSEPGQ GSTTTIKIPL TLAIIEGMSV SVGGSRFTVP
INYISRSFRP EDGAIFRDPD GSEMIMVQGK CCPVVRLYDM YGIPDAIHEP TDGILLLLET
GDSRFGVMAD ELLGVQEIVV KPVPKYISRM MKTTGISGCT LLGDGSISLI IDPQQVHNII
FD
//
