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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//