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Entry: A0A0E3S9Q5_9EURY
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ID   A0A0E3S9Q5_9EURY        Unreviewed;       620 AA.
AC   A0A0E3S9Q5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MSLAZ_3096 {ECO:0000313|EMBL:AKB76357.1};
OS   Methanosarcina lacustris Z-7289.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB76357.1, ECO:0000313|Proteomes:UP000033072};
RN   [1] {ECO:0000313|EMBL:AKB76357.1, ECO:0000313|Proteomes:UP000033072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-7289 {ECO:0000313|EMBL:AKB76357.1,
RC   ECO:0000313|Proteomes:UP000033072};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009515; AKB76357.1; -; Genomic_DNA.
DR   RefSeq; WP_048128541.1; NZ_CP009515.1.
DR   AlphaFoldDB; A0A0E3S9Q5; -.
DR   STRING; 1434111.MSLAZ_3096; -.
DR   GeneID; 24807973; -.
DR   KEGG; mls:MSLAZ_3096; -.
DR   PATRIC; fig|1434111.4.peg.4080; -.
DR   HOGENOM; CLU_000650_3_7_2; -.
DR   OrthoDB; 293137at2157; -.
DR   Proteomes; UP000033072; Chromosome.
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; 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; 3.30.565.10; 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:AKB76357.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Transferase {ECO:0000313|EMBL:AKB76357.1}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          245..489
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          491..620
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          106..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   620 AA;  70547 MW;  E94AC67984F39738 CRC64;
     MDMSKYIGIF RSESEKYIKE MSDSLLELEL DPVNIEQMNV MFRAAHTFKG MAATMGFRQI
     VELTHEMESL IERFRTGRLT LDSSLIDILF ECLDALEGLV ENVCKSAERK TEERKNDRSE
     SNKSYPDAGE VLKTLRAINN PSEEVIPRKT ESDSFSVDKK IGEKEEKKEE KERREGEEKE
     ERERKEEKKE KQEEEREKKQ LKSINEELKE NKSCTDSGPD SKVNSVQKLR IQDSKTPSPK
     IQSSRISTEQ LDKLMNLVGE LVINRSRVKE LTGESKSKDL EFALSEFQKL TRELQEEVLE
     IRMVPLDHIT NIFPRMIRDL ARAQNKKINF IIRGKEIKLD RAIMEEIVDP LVHLLRNAVD
     HGIEIPEKRV ELGKEENGTI MITASRQQNY ILIKIEDDGR GINTEEIRKA ALKKGLISRE
     EAEQLSEREV IKLIFTPGLS TASMVTDLSG RGVGMDVVKN RIERLGGTIK VESKPGSGSR
     FELRLPITIA LYQAMLVKVG MERYAIPFTS IVKSISVRKE EVRHIRGEEV IVINEKALPL
     LKLSKLFQLP AAQKEESLVI VIVEKAGQYI GLVVDALLGK QEVIIKNFKS KLLEKTRGFA
     GATIMGDGSV ILILDVNSII
//
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