ID A6GTW3_9BURK Unreviewed; 722 AA.
AC A6GTW3;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LMED105_10980 {ECO:0000313|EMBL:EDM82360.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM82360.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM82360.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM82360.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM82360.1}.
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DR EMBL; ABCT01000019; EDM82360.1; -; Genomic_DNA.
DR RefSeq; WP_008252466.1; NZ_ABCT01000019.1.
DR AlphaFoldDB; A6GTW3; -.
DR STRING; 391597.LMED105_10980; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000010322; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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: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 ATP-binding {ECO:0000313|EMBL:EDM82360.1};
KW Kinase {ECO:0000313|EMBL:EDM82360.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EDM82360.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW Transferase {ECO:0000313|EMBL:EDM82360.1}.
FT DOMAIN 3..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 309..557
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 559..692
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 50
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 722 AA; 78435 MW; 1739E4F364696987 CRC64;
MAFELDLDAS RGIFFTEARQ LLAEVESYVL QLEQNPNDTE VLNAAFRAAH TIKGSAGVFG
LLVITHFVHD LETVLDRVRN SEIGFDANMS TLVLECRDHI SELVDCIEAG GDAEHVSPDM
AVAQAGLTAR LKAYLLQEDQ PDAIQPSRPL EVNNTEQTWH VSVRLGRSTL CDGFDPAPIF
SYMETYGELQ AVIPVLDALP SFADLDAESC YLGFELRFVT DKGQAGIEDA FEFLTEESRV
RILSHSCTPE QWDALVSALP EGAARAAELL QEAGFPRPQE EALPEVMEVT GNAVTTASGK
SKATGKATPV SSFIRVPSDK LDALINLVGE LVIANAGTVE QAKHLNHTAM LESTSAVAGL
IEEIRDGALG LRMVQIGETF QRFQRVVRDT AMGLGKQIQL EISGEDTELD KSVVEKIGDP
LMHLVRNALD HGLETPEERV AAGKPATGRL QLNAYHDSGH IVIEVNDDGR GLAREKILKK
AIEKGIVTPD QTLSDTEVNM LIFAPGFSTA DKVTDISGRG VGMDVVKRNI EALRGSVQVR
SRPGNGCTFE IRLPLTLAII DGFMIGVGGS VYVIPLSYVR ECLELPVDAL GTEDRMDIHY
DLRGEFLPCV RLRKVFHPNA KRPKRENIIV VSFGGVRAGI VADYLHGESQ TVIKPLGNLF
EQNRAISGAT IMGNGDVALI IDVPKLITEV SSISTKTAEL EFSRQAIEQP AVPSQSLEQA
DA
//
