ID A0A0M2VF65_9GAMM Unreviewed; 729 AA.
AC A0A0M2VF65;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VT06_13240 {ECO:0000313|EMBL:KKO48200.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO48200.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO48200.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO48200.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKO48200.1}.
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DR EMBL; LAHP01000018; KKO48200.1; -; Genomic_DNA.
DR RefSeq; WP_046554799.1; NZ_LAHP01000018.1.
DR AlphaFoldDB; A0A0M2VF65; -.
DR STRING; 1632859.VT06_13240; -.
DR PATRIC; fig|1632859.4.peg.2742; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000034895; 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; 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:SF1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000034895};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 369..578
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 580..715
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 268..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 729 AA; 77569 MW; 970064F000515596 CRC64;
MSFDMDEDIL QDFLVEAGEI LELLQEQLVE LENNPDDANL LNAIFRGFHT VKGGAGFLSL
TELVDACHGA ENVFDILRTG KRRVTSELMD VILQTLDAIN AMFVAVQARQ PLTPANAELL
DALHYYSEPA SEGSAPPVVE AAPEPNAAID SGDIDDISEA DFEKMLDELH GKGAPGRNEA
VPTPVAASTS SALNTAENSD ITDDEFEAIL DQLHGKGSFV PDSNTTAGVA ANAGKTAVTP
TANTTSVKTD EISDDEFEAL LDQLHGKGNA PVEVAPPAPR KPAPVAPVKP TQAAASTPVA
PVKAPVAANA PAPSSAPAAA NADKAAAAAE TTVRVDTKRL DQIMNMVGEL VLVRNRLVSL
STSTQDEAMT KAISNLDVVT ADIQGAVMKT RMQPIKKVFG RFPRVVRDLA RALQKDINLV
LEGEETDLDK NLVEALADPL VHLVRNSVDH GIEMPDVRLK AGKPKVGVVK LAATQAGDHI
LLTIEDDGAG MDPEKLKGIA IKRGILDVDA AARMSDNEAF NLIFAPGFST KEQISDISGR
GVGMDVVKTK INQLNGTVQI NSKLGQGTLL EIKVPLTLAI LPTLMVMVGA QTFALPLAGV
NEIFHLDLAK TNIVDGQLTI VVRNKALPLF YLEHWLVKGS NKQLRREQGH VVIVQIGTQQ
VGFVVDSLIG QEEVVIKPLD ALLQGTPGMA GATITSDGGI ALILDVPNLL KHYAKKSKIK
FDRFNKLNA
//
