ID A0A0Q5Z8Y2_9BURK Unreviewed; 1985 AA.
AC A0A0Q5Z8Y2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG30_00810 {ECO:0000313|EMBL:KQT14161.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT14161.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT14161.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT14161.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT14161.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT14161.1,
RC ECO:0000313|Proteomes:UP000051173};
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 -!- 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:KQT14161.1}.
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DR EMBL; LMQL01000001; KQT14161.1; -; Genomic_DNA.
DR RefSeq; WP_055891165.1; NZ_LMQL01000001.1.
DR STRING; 1736365.ASG30_00810; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000051173; 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; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001789; Sig_transdc_resp-reg_receiver.
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; 3.
DR Pfam; PF00072; Response_reg; 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; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 3.
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; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT DOMAIN 647..751
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1008..1110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1205..1305
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1457..1690
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1692..1828
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1863..1979
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1378..1433
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 694
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1054
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1251
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1912
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1985 AA; 213054 MW; 728320BAC6ED2028 CRC64;
MQANDNDLDL ATNDLGPLAW VLDELRKSLE SASAALRRFV RDAGLARGQD MASVDTGQLR
IARQQLHQAV GALEMVGLGA PALILRAMEA SVQKFVERPE LCSEPAAAKV ERAGFALTEY
LEGVLLGKAA SPVALFPQYK DVQELAGSDR IHPADLWPFD WRWVEAETPA VARKLVYDPA
LRSRMDQAVL RVVKTTDPAA GKELAECCLG LAAGQEARQP RIFWKIAAGY FEALALGLLP
ADLYVKRAAS RVLTQYATLA KGELGVSDRL AQDLLFFCAQ AVPPRVVDGP VLAGVRASYA
LQRFTPIDYG TPHYGRFDPV LLTQARKRIT AAKESWSAAS GGDVTKFKVL GEQFHLIGES
LTKLHAPSAP LAQSLVATVD TVVRSAQPPR AEVAMEVATA VLYLEAAFQD LDPADSQLAL
RTARLAERLD GVRQGGQAEA LEAWMEELYR RVSDRQTMGS VVGELRGTLG ELEKLLDAFF
RSPQEKGPLK NAPTHLLQMR GVLSVLGLDQ AAHAVARMRE TVEQILIGDF DEDAVLRAST
FDKLGNNLGA LGFLIDMLNY QPALVKKLFI FDDTRGELRP LMGRAEAAKP TFALPTELPS
LEIAPAVELV APAAAIAVAP QVPVAVPPAP AVAGAAPMAP AAADTGADET DDELREIFLE
EAREVVGNGL AAVEALAAQP SDVAELTTLR RAFHTLKGSS RMVGLNEFGE AGWALEQVLN
TWLADQKPAS EDLRTVSAEA LRGFGRWIED IAAGTDAGWK SGMFRGPADV LRTEGRVLPF
PFPGAAVEAA TAQGGLPALE IDFGAPAAAI EPALESLDLA PQAAPEAIEL SVPSFDFDLT
PSEPVSAEPV ALVPAQADPL ADFDLVIAEA AAAQDDAEAF GNTHVIRGQA VVAEEITLDE
LPADFAAELG PAAPVGDLAP TTSPAEAEIS AVDFDSLSAL ALAQAPELLP EAPEAPEAPS
FDLPEFDLPP TVATATAAPE PEPEPLASDS AFVDSQMPVD DQIKVIGGLR IGIPLYNVYL
NEADEWSRRL SQELAEWALE LKEPLSDTAV GLAHALAGSS ATVGFHALSD IARALENSLQ
HAQTLAWGTP QHGRAFVEAA EEIRRLLHQF AAGFLKEADP GITQSLQALE ALQLPKRAEL
RDSGSGELEG MDFAAPVEEA PAAPLAKPAS KVVHFPTLHA AAATAAPGAA AQGSRLSGDD
DIDAVDAIDP DLFPIFEEEA VDLLPKLGAG LRQWAQQGVR EGRDEVLRVL HTLKGSARLA
GALRLGEMAH RMESAIEGLP AETPAADLEP LLQRFDDLQG AFDTLRVRAS EPEAEPAPAA
QPQAPVEIAP VALQQAMPQP SVQQPAPQRA LLAAPVTTTL TPQRAAANQA VRVRSQLLDR
LMNQAGEVMI TRSRLENELR NLRGSLNDLT GNLDRLRSQL RDIELQAETQ MQSRLAQAKD
SAGFDPLEFD RFTRVQELTR MMAESVNDVA TVQRNLQRTV EATEDDLIAQ ARQTRELQRD
LLRTRMVEFE GISDRLYRVV RLASKESARQ VKLDITGGSI EMDRGVLDRM TPAFEHLLRN
CVAHGIEDVA VRQAAGKDAA GTILIDVRQE GNDVSVEFRD DGAGLNLARI REKALQQGLV
TPDQQLSDAD AANLIFTPGF STAAQVTELA GRGIGMDVVR SEVNALGGRI ETSTQAGRGT
SFRLVLPLTT AVTQVVMIRS GNLSIGVPAN LIEVVRRAPA REVQQAYNSG VFDFGGEQVP
FYWSGALLQS SQRSAEPQAK TLPVVVFRSA AQRVAVHVDE VLGNQEVVVK NLGPQLARLP
GLAGMTVLAS GAVVLIYNPV ALSSVYGERA RRLSADHAQP EMLEQAGQPA VPQLAPAAPQ
IPLVLVVDDS ITVRRVTQRL LQREGYRVAL AADGLQALER LAEEKPAVVL SDIEMPRMDG
FDLARNIRAD ERWGQLPIVM ITSRIAEKHR EHARELGVNH YLGKPYSEEE LLSLVKHYCT
AAVAA
//
