ID W5IMT2_PSEUO Unreviewed; 746 AA.
AC W5IMT2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PM1_0229835 {ECO:0000313|EMBL:ETM64715.1};
OS Pseudomonas sp. (strain M1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=95619 {ECO:0000313|EMBL:ETM64715.1};
RN [1] {ECO:0000313|EMBL:ETM64715.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM64715.1};
RX PubMed=10388678;
RA Iurescia S., Marconi A.M., Tofani D., Gambacorta A., Paterno A.,
RA Devirgiliis C., van der Werf M.J., Zennaro E.;
RT "Identification and sequencing of beta-myrcene catabolism genes from
RT Pseudomonas sp. strain M1.";
RL Appl. Environ. Microbiol. 65:2871-2876(1999).
RN [2] {ECO:0000313|EMBL:ETM64715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM64715.1};
RA Soares-Castro P.M., Santos P.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETM64715.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM64715.1};
RX PubMed=23405299;
RA Soares-Castro P., Santos P.M.;
RT "Towards the Description of the Genome Catalogue of Pseudomonas sp. Strain
RT M1.";
RL Genome Announc. 1:E00146-E00112(2013).
RN [4] {ECO:0000313|EMBL:ETM64715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM64715.1};
RA Soares-Castro P., Santos P.M.;
RT "Decyphering the genome repertoire of Pseudomonas sp. M1 towards myrcene
RT biotransformation.";
RL Submitted (DEC-2013) 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:ETM64715.1}.
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DR EMBL; ANIR02000003; ETM64715.1; -; Genomic_DNA.
DR AlphaFoldDB; W5IMT2; -.
DR eggNOG; COG0643; Bacteria.
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 InterPro; IPR037257; T2SS_E_N_sf.
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; SSF160246; EspE N-terminal domain-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 Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 3..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 341..582
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 584..714
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 715..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 746 AA; 80590 MW; E09A7D34D1690603 CRC64;
MLDGEQWSEL LRGFIEEARD LARQAEECLL ELERNPADGE AITRLFRAMH TLKGSAGLFS
LLPLVNFTHH LENLLMAVRD GERALTAELV SLMLRCLDEI TSMVALIDPA SGELPVDAAH
QRELLDALAA LTGNEPELIP TQAIDCPARG RLDACASCEA QGAWHISLRF DGELLRNGFD
PATFVRYLGR LGEVLCLHLI DDAVPALEEL DAERCYLGLE IALCTSAERA AIEEAFEFIR
DFCSLRLLPP GSQVDDYLAL MRELPESDER IGAILVASGL LDEQDLARGL ALQAQHSDAL
KPALGSVLVD QGLVPAQAVN AALAQQQKAR ERAPESSLIR VAAHKLDELI NLVGELVISA
AAAQLHARAS GDSASSESAQ TVNRHVELIR EAALKLRMVE IGETFSRFHR VVRDVSQQLD
KRIRLEIHGA DTELDKSVID KLADPLTHLV RNAMDHGIEP AGQRIEAGKA PEGLLRLNAF
HESGTVVIEV SDDGRGLDTR RIRAKAVERG LIEAGATLGE QELQRLIFAA GFSTADSVSD
LSGRGVGMDV VRSAIEALRG SIEIDSRAGQ GSTFRIRLPL TLAIIDGFQV SLGDEQFVVP
LGLVTECMEL PPHAGDGACG YIDLRGRPLP CIDLAAHFGL PGSRGGRRNI VVVSHGRQQA
GLVVDHLHGE LQTVIKPLGP LFQHLQGIAG STILGSGQVA LILDIATLFA SLDEQPTHHP
VDSDPQQSHR HPQAAGAQET PHEIHP
//
