ID A0A0Q6BPL4_9PROT Unreviewed; 795 AA.
AC A0A0Q6BPL4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG34_00025 {ECO:0000313|EMBL:KQT43236.1};
OS Methylophilus sp. Leaf416.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT43236.1, ECO:0000313|Proteomes:UP000050891};
RN [1] {ECO:0000313|EMBL:KQT43236.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43236.1,
RC ECO:0000313|Proteomes:UP000050891};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT43236.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43236.1,
RC ECO:0000313|Proteomes:UP000050891};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- 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:KQT43236.1}.
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DR EMBL; LMQS01000001; KQT43236.1; -; Genomic_DNA.
DR RefSeq; WP_055824931.1; NZ_LMQS01000001.1.
DR AlphaFoldDB; A0A0Q6BPL4; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000050891; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.70.400; CheY-binding domain of CheA; 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; IPR015162; CheY-binding.
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; PF09078; CheY-binding; 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 428..634
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 636..771
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 130..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 795 AA; 84351 MW; 4CEC5013D51174D9 CRC64;
MTVDMSQFYE VFFDEAEELL AEAERLLLNI DVDSPDIEEL NAIFRAAHSI KGGAATFGFM
DMAGITHVLE NLLDKIRKQE MALTMEHVDA FLAAKDVIKM QLDGHRHGSE VDAAQVDEIS
ATLKALSEGK TEAPAPAAAA PAAPEPAIQG STPAPALTAT AEEQASGIQV YDVGLPEVTE
KDLDNLKDEL ALLGEVAIYK RGDKHALLVK TDSSADDIIS ICSFIVDPDA LVVKVAGAEA
PAAEPAPAAE VAAEAAPADA APVEADLGYG FFDSEPVSAD AKPAQAASAD GKVAVAEEVG
YGFFTNSGEE PQEEGYGFFA PFKPHPDAPK AQMIGDDNAA AALAKASSEA EAKAATNAPP
AEVKEDRRAQ SRRESDKPAA PQNAESSSIR VGIEKVDQLI NLVGELVITQ AMIEQRVNAL
DPTDNEGLIN SVSQLTRNTR DLQESVMSIR MMPMDFVFSR FPRMVRDLAG KLGKKVEFVT
NGATTELDKS LIERIVDPLT HLVRNSVDHG IEKPEVRREL GKSESGTLTL SAAHKGGSIV
IEVTDDGGGL NRDRILAKAA SNGLPVNESM SDSEVYSLIF APGFSTAEVV TDVSGRGVGM
DVVKRNISAM GGNIEIRSAL GYGTTISISL PLTLAILDGM SVSLGKSLYV VPLNLIVETL
QPRAEDLKTV TGEGLMVHVR GEYLPIIALH ALFNHPTEIT APTDGVLLIL EADGKKSALF
VDRLVGQQQV VIKSLETNFK RIPGVSGATI MGDGSVALIL DVPAITQMGQ TTNYITGGRS
FADQNYSNLQ NHINA
//
