ID A0A316HVH9_9GAMM Unreviewed; 1989 AA.
AC A0A316HVH9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7456_11043 {ECO:0000313|EMBL:PWK84742.1};
OS Fulvimonas soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Fulvimonas.
OX NCBI_TaxID=155197 {ECO:0000313|EMBL:PWK84742.1, ECO:0000313|Proteomes:UP000245812};
RN [1] {ECO:0000313|EMBL:PWK84742.1, ECO:0000313|Proteomes:UP000245812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14263 {ECO:0000313|EMBL:PWK84742.1,
RC ECO:0000313|Proteomes:UP000245812};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWK84742.1}.
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DR EMBL; QGHC01000010; PWK84742.1; -; Genomic_DNA.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000245812; 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; 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; 4.
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; 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:SF8; HISTIDINE KINASE; 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; 4.
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; 5.
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}; Kinase {ECO:0000313|EMBL:PWK84742.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000245812};
KW Transferase {ECO:0000313|EMBL:PWK84742.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 670..777
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 861..965
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1212..1316
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1465..1698
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1700..1837
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1862..1979
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1003..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1397..1431
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 717
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 905
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1259
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 1989 AA; 214646 MW; 3ACBAF0C60DDD610 CRC64;
MRLQEHIDFT TLQWVKPELD ETLARAREAL ESYVDNPGNP APMRACVDHL HQVQGTLRMV
ELYGAALVAE EMETLAISLL EDHVRQREEA YAALMRGLMQ LPDYLERLSG GHRDVPVVLL
PLLNELRASR DQQALSEAAL FTPNLEAALP AQLPGAADEA EAERRLGEIA DLRVRFQQHL
LAWFRGQNPA QQLAGMRQAL LAISARCWSV PGRRLWWITA GVLEGLEQGL LKSQAGEVRQ
LVGKVDRNIR QLLDQGEESL RGGDADDLAR KLLYIVAQAK QRSPQMELLR QTYRLDSLLP
DAGELEHARG SMSGHNRALL DSVAKALKED LLRVKDALDL FLRQQGADPA SLSAQGEVLE
RVGDTLGMLA LAVPRRVINE QRRVLEEIAQ RVRPVEEETL LDVAGALLYV EASLDDHIES
LGAEESAAEE IAPVLPRSEA RHILATLMQE AIGNTSRVKE AIVAFIESGW QHAALAGVPA
LMGDVAGALR MLSAMRPAEL AEGIGRFVGN ELLADRRVPG SQQMDHLADA LAALEYYLEA
AREHRGGLDH ILDVAEHSLG ALGYWPLPEA RPAVQEEAAP AEAAAPPPAL SEPVSLLPGD
DLSGLFLGAE AEPAAAPAHD LDGLRLAQTG ESAPEPVAGG EDWEEIEEEV FEEVPAADPL
AASTGFQLSA EGIDDDIREI FLEEMQEEID NLQAAEQAWL ADPAQLSALV PIRRSFHTLK
GSGRLVGAAV LGEFAWKVEN MLNRVLDETI QPHEGVQALV RHAIAALPQL HVALKGGAAP
TAPLSAIMQA ADRLAAGEMA TVEQYATGGG TQTVRRVVRR LVPRLDSAAE AVPAAAFTDA
TAAPAREPAP AAEEAIPLPA MPPVDPVLLE ILRSEVAQYL QTIRTALSRS EGELPVDDGL
LRAVHTLHGA IAMVDIELLT RLLSPLEGLL KRLRAAGEPL SVEGVGLLSR AADVVDQVMA
QFDVPDPQLP DVEPLVARFT ELRDARPEPQ VAHVLFEPHA EVPEEGEAAV AEPAAAAPAD
EPAAAEDEDG HDELEAQLLA ALDSFDPATA TSLGEDGAAA DAGDEELDAL IDGLLEEPAP
EEAGLSAADE AAPEPAEASA DAGAAPEPFE ALPEELAASA GAEPAVAEPS EAGQPEIEAP
GSGIAQHEAP AVEASEVAEA PEPTEPSESA EPSEAAEVPE AEPQPQVEAL AERPAAAPVP
SAVPAPVGEI WTGQIDPDLL EVFVEEARDI LDHADGLLAQ WRTEPAELAH VVDLQRDLHT
LKGGARIAGL VPVGDLAHAI ETLLEKPIVG GQEQAVGVIR ALESGFDRLH ALVQRIGQGQ
AIEYPQDLID RFLGMAGEES LAGHEEAPAA PLAALPELLP EEQPEDEARS PQQEQIRVRA
ELLDSLVNHA GEVAIYRSRL EQQVSAYRFN LVELEQTVSR LRSQLRMLEI ETEAQIIARY
QREHREAGIA AFDPLELDRF SQLQQYSRAL AESVSDLVSI QNMLDELTRQ AETLLIQQSR
VSADLQEGLL RTRMLPFDTM VPNLRRTLRQ AAQEEGKLAQ LFVDGAHGEM DRNLLDRLKA
PFEHMLRNAI AHGIEPPAER RRAGKPEEGA VRIRVAREAT EVVVRVSDDG RGLDREMVRK
RAIERGLLRA DARPSDDQLL ALITQPGFST ASTVTQLAGR GVGMDVVANE IKQLGGSLAV
ESQPGQGTTF VLRLPFTLAV TQAILVRIGE TTFAIPMTSV QGVARISPSE LAARMAEDSP
IFDYNGEAYG IHDLSELLGL PPGHSAEDEQ LPLLLTRAGD LRAAIRIDAV IGSREIVVKS
VGPQISSVPG VLGATIMGDG SVLIILDLAP LVRHGVARRE QRLAEGLAAP APVAEESRVR
PLVMVVDDSI TMRKVTSRVL ERHEYEVSTA KDGLDALEKL HEARVPDLML LDIEMPRMDG
YELATQMKAD PRLRGVPIIM ITSRTGEKHR QRAFDIGVDR YLGKPYQEAE LLAQIGEVLE
QRAMELANG
//
