ID Q46DT7_METBF Unreviewed; 598 AA.
AC Q46DT7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mbar_A0984 {ECO:0000313|EMBL:AAZ69955.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ69955.1};
RN [1] {ECO:0000313|EMBL:AAZ69955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ69955.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Anderson I., Richardson P.;
RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL Submitted (JUN-2006) 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};
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DR EMBL; CP000099; AAZ69955.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46DT7; -.
DR STRING; 269797.Mbar_A0984; -.
DR PaxDb; 269797-Mbar_A0984; -.
DR KEGG; mba:Mbar_A0984; -.
DR eggNOG; arCOG04403; Archaea.
DR HOGENOM; CLU_000650_3_7_2; -.
DR OrthoDB; 293137at2157; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd00088; HPT; 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; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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 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; 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 Kinase {ECO:0000313|EMBL:AAZ69955.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:AAZ69955.1}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 195..467
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 469..598
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 140..190
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 598 AA; 67381 MW; 12DE0B8BF0ACAF41 CRC64;
MDMSKYMDIF RVESEKYIKE LSDSLLVLEN DPENTEQVNT LFRAAHTFKG MAATMGFKQI
VELTHEMESL IDGLRTRQTV LNSSLIDVLL ICVDTLEGLV ENVCGSEGNK PEKEKKDSVN
KYEYHPDVYE VLKTLRKVND SPEKASIQKA GDKSLSAEKK SEEGGEESGK IKDNAKKCNR
DNEVSKTEET NKVKNAAKEI YLPEKAPAYP KSSPKVKIVQ NPRISTKQLD KLMNLVGELV
INRSRINELT RDLKSKELEA ALSDFHKLTR ELQEEVIEAR MVPLDHITYI YPRMIRDLAR
VQNKKIDFII KGKEIKLDRT ILEEIGDSLV HLLRNAVDHG IEIPEKRVEL RKKENGTVLI
TASRQENFVL IRIEDDGCGI DTNEIRKVAL KKGIISRESA EQLQEEEAMQ LIFTPGLSTS
DNVTDISGRG IGMDVVKNRV ERLGGSVKVE SKPGLGSSFE LKLPLTVAVY QAMLLRVGKE
KYAIPFTSIV KNIEVSSQEI KHIKGQEVIL IDNKILPLFR LKRQFQLPDD DDENNIFVVL
VEKHGQYTGI IVDELLGKQE VIVKSFKSKL LDDTRGFAGA TILGDGSIIL IIDVNSLI
//
