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Database: UniProt
Entry: M5E3D8_9FIRM
LinkDB: M5E3D8_9FIRM
Original site: M5E3D8_9FIRM 
ID   M5E3D8_9FIRM            Unreviewed;       660 AA.
AC   M5E3D8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HSACCH_02324 {ECO:0000313|EMBL:CCU80805.1};
OS   Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU80805.1, ECO:0000313|Proteomes:UP000012063};
RN   [1] {ECO:0000313|Proteomes:UP000012063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX   PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA   Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT   "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT   Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL   Genome Announc. 1:217-225(2013).
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}.
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:CCU80805.1}.
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DR   EMBL; CAUI01000023; CCU80805.1; -; Genomic_DNA.
DR   RefSeq; WP_005490076.1; NZ_CAUI01000023.1.
DR   AlphaFoldDB; M5E3D8; -.
DR   STRING; 1293054.HSACCH_02324; -.
DR   eggNOG; COG0643; Bacteria.
DR   InParanoid; M5E3D8; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000012063; 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; 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: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, ECO:0000313|EMBL:CCU80805.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012063};
KW   Transferase {ECO:0000313|EMBL:CCU80805.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..103
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          276..524
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          526..660
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   MOD_RES         46
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   660 AA;  73887 MW;  98B8D2E88BD738B5 CRC64;
     MQENEYLKIF FAEAKEYIEV LNNGILTLEN NPEDKETIDA IFRAAHSLKG MAAAMGFEKL
     TELTHKLENS LDKIREGEIK VKTEFIDLLF QALDNIQYLV KAVEENNGKE PEGFDLDALI
     AELNAYTEAN DFKESQTAAV DTSENVRDFL TEAEKEELLE RKKDKEKVYH LKAEVVDEEF
     KSVRAFMLLK KLDEIGQLFK SEPPRNTIEN SEADIDQLNI IALSWLEKEE FKTEIEAQSS
     IKLISLDELQ SSEIKIDSEK ESKSNTVQKN KVSSFNSSST VRVDISKLDT LMNMVGELLI
     NKSRLESLDI KKTKFKEIMP QLDRVTMDLH HIVMQIRMVP VGVMFSRFPR MMRDLANKMN
     KEIDFVMSGQ ETELDRSIID ELADPLTHLL RNAIDHGIEK PAARKAAGKD GKGKVELLAY
     QKGSEIIIEV KDDGAGIKAA AIAKKAVDKG IIEQEEVEQL EKRDILDFVF HPGFSTAQEI
     TDVSGRGVGM DIVRSTVKKL DGQVSIDSEP GEGSTFKITL PLTLAISQAL MVKIIGDTFA
     IPLSAVSETL TIETENIKKI RGKDVIVLRE TTIPIVSAAA IFGDDDQKSF KNSEKDLSVV
     ILKSGERKVG LVVEELLNQQ EIVIKSLGKY LQETRYISGA TIIGDGDVAL IVDVRDVVSR
//
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