ID W9VBQ1_9GAMM Unreviewed; 739 AA.
AC W9VBQ1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D779_2455 {ECO:0000313|EMBL:EXJ16844.1};
OS Imhoffiella purpurea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Imhoffiella.
OX NCBI_TaxID=1249627 {ECO:0000313|EMBL:EXJ16844.1, ECO:0000313|Proteomes:UP000019460};
RN [1] {ECO:0000313|EMBL:EXJ16844.1, ECO:0000313|Proteomes:UP000019460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK35 {ECO:0000313|EMBL:EXJ16844.1,
RC ECO:0000313|Proteomes:UP000019460};
RA Nupur N., Khatri I., Subramanian S., Pinnaka A.;
RT "Genome assembly of Thiorhodococcus sp. AK35.";
RL Submitted (NOV-2012) 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:EXJ16844.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AONC01000004; EXJ16844.1; -; Genomic_DNA.
DR RefSeq; WP_043748657.1; NZ_AONC01000004.1.
DR AlphaFoldDB; W9VBQ1; -.
DR STRING; 1249627.D779_2455; -.
DR PATRIC; fig|1249627.3.peg.410; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000019460; 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 Kinase {ECO:0000313|EMBL:EXJ16844.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000019460};
KW Transferase {ECO:0000313|EMBL:EXJ16844.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 391..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 593..727
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 739 AA; 80506 MW; 70FD205F99AB2F07 CRC64;
MNLEDARQAF IGEVAELLDS MEDALLTLEE DPQDSESLNE VFRAMHTIKG TSGVFGYAPV
VEFTHAVETL MDQVRSGQRP LTKPLIATLF ECRDHTARLV EVIEEQGPDG DEEVQFGEVL
REAGESLLQR LGQSGATSPM ASAERPADGA ADKRLPVSSE LWMITLEFGA DAFRNGMDPL
SFLRYLGSLG DLVHVSTLLR LDPSQEEGFD PESCYLCFGI AFRSDADKQT IAGVFEFADQ
DCEIRILEPE STHSRYMELL ESVAEDEVGC IGELLVQVGA LTRRELERAL QIQETETSAC
SMTSCSNLRR RLGEILVEQG SVKSAVVEQA AKTQETVRAR RQDESRFIRV DAQRLGHLID
LVGELVTSSA AIRVMVNRAG IDDATEVVDG VDYLVSEIRD SALQLRMVPI EECLSRFRRV
VRDASQELGK QIDLVITGGE TELDKTVIER LTDPLTHLIR NAVDHGIETP DVRAGRGKPA
SGTIHINAFH DSGHIVVEIA DDGAGLDPAR IRAKAEARGL VKPDDSLRED EVLRLIFAPG
LSTKEEATNL SGRGVGMDVV RSNIEALRGS VELDSSPGVG TKVTIILPLT LAIIEGFLVG
AGEDRFVIPL SQVAECVEME AADALHRRGR HYINLRGEVL PFIRLAEIFE SGGTREAGRR
ESLVVVRFGH HKMGLVVDSL LGELQTVIKP LGILFERLRG VAGATILGTG DIALILDVAE
LAAVDQGARS PSGSARATR
//
