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Database: UniProt
Entry: A0A1G3KPG8_9SPIR
LinkDB: A0A1G3KPG8_9SPIR
Original site: A0A1G3KPG8_9SPIR 
ID   A0A1G3KPG8_9SPIR        Unreviewed;       736 AA.
AC   A0A1G3KPG8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-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=A2Y41_01430 {ECO:0000313|EMBL:OHD07465.1};
OS   Spirochaetes bacterium GWB1_36_13.
OC   Bacteria; Spirochaetota.
OX   NCBI_TaxID=1802174 {ECO:0000313|EMBL:OHD07465.1, ECO:0000313|Proteomes:UP000177420};
RN   [1] {ECO:0000313|EMBL:OHD07465.1, ECO:0000313|Proteomes:UP000177420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(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   -!- 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:OHD07465.1}.
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DR   EMBL; MIAO01000136; OHD07465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3KPG8; -.
DR   STRING; 1802174.A2Y41_01430; -.
DR   Proteomes; UP000177420; Unassembled WGS sequence.
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; 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   InterPro; IPR037257; T2SS_E_N_sf.
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; SSF160246; EspE N-terminal domain-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   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110}.
FT   DOMAIN          140..247
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          383..591
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          593..728
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   MOD_RES         187
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   736 AA;  84246 MW;  92107EDF94FF6AD4 CRC64;
     MKKFKSEFAQ NKKNELFSSV NLIINKVENL ENGDLFLISE IKEDFENLQK QIEKNSSIEC
     CLQDFAFLIE AFLFTNENEA IKKSALESLK DIILFYKNEI DINILNKKHD QRNQKINQIK
     EKMQLNESLS DKYSKNYFNN IIQDEKMLSQ LCDEINDHMN KAQYTLVDLE YDETNQENIN
     KIFRAFHTAK GSSAFLGLKN IEEVGHQMEN LLVLVRDGKL RITSELIDVI FIGIELLRNL
     TSIMEVNQFK IEKMVESFKK VDIFSYIRLI KKILEQYSFK KIGQILEEEG LLRVKDVKHI
     LQKQKETSKK FGEIAVEEKM ITPTELENAV NKQTSSLKKS SYVRVSNDRL NLLVDTVGEL
     VINQSMLRQI LTDSKMDNKA VRERVISQLE GISTNIKNIV LSMGMVPIAE VFNKLRVVIR
     NTTTELGKAV IVDIRGEDTE LDRNVIETIY DPLVHIVRNA VDHGIEFPGE REKGKKDRVG
     KIIISAEHKG NGIEISVWDD GKGIKKERII EKALQLGLLG EDKIENLTEK EIYNLMFQPG
     FSTAEKVTEV SGRGVGLDVV KKNIDEIRGK IEIFSKEKEF TKFVIKLPLT LAIIEGFVTE
     VGENKYIFPF NLVDEIIVPQ EEMLSIMDNG TMMLFNRGIY IPVIFSGKIF GESEYKKDTN
     NLVAIIIFYD NKHYAVVVDK VIGKQETVIK NLSEVLNDLA VFSGGTIFGD GTIGFVVDLD
     GFLDKVKDLE EKIKKN
//
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