ID I3CYZ7_9BURK Unreviewed; 734 AA.
AC I3CYZ7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GWL_01290 {ECO:0000313|EMBL:EIJ48840.1};
OS Herbaspirillum sp. GW103.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1175306 {ECO:0000313|EMBL:EIJ48840.1, ECO:0000313|Proteomes:UP000004194};
RN [1] {ECO:0000313|EMBL:EIJ48840.1, ECO:0000313|Proteomes:UP000004194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW103 {ECO:0000313|EMBL:EIJ48840.1,
RC ECO:0000313|Proteomes:UP000004194};
RX PubMed=22815460; DOI=10.1128/JB.00806-12;
RA Lee G.W., Lee K.J., Chae J.C.;
RT "Genome sequence of Herbaspirillum sp. strain GW103, a plant growth-
RT promoting bacterium.";
RL J. Bacteriol. 194:4150-4150(2012).
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:EIJ48840.1}.
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DR EMBL; AJVC01000001; EIJ48840.1; -; Genomic_DNA.
DR RefSeq; WP_008325493.1; NZ_AJVC01000001.1.
DR AlphaFoldDB; I3CYZ7; -.
DR STRING; 1175306.GWL_01290; -.
DR PATRIC; fig|1175306.3.peg.125; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000004194; 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: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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EIJ48840.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transferase {ECO:0000313|EMBL:EIJ48840.1}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 379..584
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 586..716
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT COILED 370..397
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 734 AA; 80059 MW; C7D77DC6220E0E5D CRC64;
MKKDSARDAV VQEARELLVA MEAALLQIEM EGPSRDSINA IFRAAHTIKG SAGLFAFDSI
VQFTHQVEHV LDLVREERLP LNAYMMSLLL QCGDYIGELV DAIERNQEAE EPNAERRATL
LAELDEVAQS AIASRELVSG QPTLVGQRLA GSPAADPLAT DEASMDATLQ AAADYPYWHL
SLQFNENVLR DGLDPLSFLH YLRSLGRIVA ILPVEAGMPA AAAMDAESCY LGVEICLVSD
STRQTLEDVF EFVRDDSRID ILPPHSPLCA YAAVLQRLAR EDAARLAGQW RSLSLFNEVQ
WRCLGAVTLE EAVAAVVPAA TDAGARPRPL EERRAQEQKF IKIEVSKLDQ LIDLVGELVI
AGASARLIAR RRKDSQFEEA TQAIDSLMEQ IRDAALTLRM VQINEVFQRF PRIVRDIARD
LDKDIELTMT GSETELDKSM VERLADPLMH IVRNAIDHGI EPAAERIAAG KPAKASLRLN
AMHESGSVLV EVMDDGRGMD RARILEKAIA QGLAAPDAEL SDGEIFRFVF EPGFSTAQQV
TELSGRGVGM DVVKRNIDVL QGEVGIDTEP GRGTVVRIRL PLTLAIISGF QVVVGNAVFV
IPLDMVVECI DMPPRQSGSH IVSVRGEPLP FVPLRELFDL PARDQGRGRK SLVIVQYGQL
RAGLLVDGLL GECQAVIKPL GRLFGKVKGL SGSTILGDGR VALILDIAHL VQHTQQQEQG
NTAAYAESSV ASAP
//
