ID M9M778_GLUTH Unreviewed; 683 AA.
AC M9M778;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NBRC3255_2297 {ECO:0000313|EMBL:GAC88636.1};
OS Gluconobacter thailandicus NBRC 3255.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1291534 {ECO:0000313|EMBL:GAC88636.1, ECO:0000313|Proteomes:UP000011890};
RN [1] {ECO:0000313|Proteomes:UP000011890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3255 {ECO:0000313|Proteomes:UP000011890};
RX PubMed=23580707; DOI=10.1128/genomeA.00118-13;
RA Matsutani M., Kawajiri E., Yakushi T., Adachi O., Matsushita K.;
RT "Draft Genome Sequence of Dihydroxyacetone-Producing Gluconobacter
RT thailandicus Strain NBRC 3255.";
RL Genome Announc. 1:e0011813-e0011813(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 -!- 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:GAC88636.1}.
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DR EMBL; BAON01000019; GAC88636.1; -; Genomic_DNA.
DR RefSeq; WP_007283814.1; NZ_BAON01000019.1.
DR AlphaFoldDB; M9M778; -.
DR Proteomes; UP000011890; 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110}.
FT DOMAIN 6..110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 305..539
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 541..675
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 271..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 683 AA; 76478 MW; F953DE60333BDB30 CRC64;
MNNYVETDDL ESIRLIFFEE CGEQLSLLEE ELSSLDAATG PGEKINTIFR AVHSIKGGAG
AFGMEKLVRF SHLFEAVLEK FRGGECTVDQ AAIATFLKAA DVLTDIVAFY RDGTDLSVQD
DVVEELDRYI NVPEALSKSP VSVEELPEDI EGISFTPIKI DLPKKEKFLL EITPRIGLYE
SGDDIRNILS FLEKKGEMEV EIHCDDLPNI EEFNVNKTYS TWNIVIFSNE NKNSLEEIFE
WSGDNIKVEF LEEKHVSCKL AGKIPNNFDK NKVDEFSGAQ KPSRDSRKEN PTIRVDTKRV
DKLVDLLSEL VINQGAIRSQ MKVNDIRPGS ALDIVISELD QLTHELQENV MAMRAHPIKT
VFQRMGRIVR ETSRVSGKDV ILHLEGEDTE VDRSILEKLS DPLTHMVRNA IDHGLESTHL
RVAAGKPAEG QLSLRAFHRS GRIIIEIEDD GAGLNCEKIH QKAISKGIIN NSILMEKEEI
QNLIFEPGFS TVENVSDLSG RGVGMDVVRK SISEIGGRIS ILTEEDKGTL FSISLPLTLA
VVEGLIFRTQ KQNFIVPVSG VVEAFLFQES KKFKISEDVW GYPYRDEYIP IINSENLTEK
NKIETKNNSC LIIENEKKEK IALIVDEIID QSRFVVKSIE KNYKKISGFS SATILGDGGV
ALIVDVDFLI ESVSGKKNVR AAK
//
