ID I4W9X5_9GAMM Unreviewed; 1221 AA.
AC I4W9X5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=UU5_07473 {ECO:0000313|EMBL:EIL96266.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL96266.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL96266.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL96266.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(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:EIL96266.1}.
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DR EMBL; AJXS01000183; EIL96266.1; -; Genomic_DNA.
DR AlphaFoldDB; I4W9X5; -.
DR PATRIC; fig|1162282.3.peg.1433; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000004557; 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; 2.
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; 2.
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; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 2.
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; 2.
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; 2.
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; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EIL96266.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EIL96266.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 32..136
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 438..542
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 698..931
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 933..1070
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1096..1212
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 485
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1145
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIL96266.1"
SQ SEQUENCE 1221 AA; 131204 MW; 40FDB374098C7B28 CRC64;
NAIPAASLAG VEAAPEPASA SSADETLPGP VLPPVDPVLL EILRSEVAQY LQTIRTAVAR
VDGELVVDDG LLRAVHTLHG AIAMVDIPLL TRLLSPLESL LKRLRGAGHP LSTEGVPLLG
RSADVVDQVM AQFDAAQPQL PDADALTARL AELRDQEPEP QVAHVVFEPQ DDEIAAVDTV
QAGPEAPESH EPVRDDESDY DDHAADLEAA LAGFDIDTAE PLPASPAAQS KDADDEDFAA
LLASLDEVLE PAGHGAASTP ALEAFDAHAG EGEAHDEATA DAETPVEARD VEAADAGELT
DAAAEISAPA DEATVVDESA VAAEVPSAPD EIAAEAEPSE AVHHGIHEPV VAAAETVDSD
AAKPVEEVAS EPEPVDDVAD VASDITEPSA TTAPTEAEHE HAPVEPAAVP AEPSAVPAAP
VVTARVVVPA ETGPEISFGE IDPDLLEVFG EEAHEILDQS DAVLAQWRVE PDESAHVASL
LRDLHTLKGG ARISGLAPVG DLAHAIETVL EHPPEAGSPQ VPLLIATLEV AFDRLHDLVQ
RVTHGHPIVY PQAMIDHLLA WTGKAPVATE AGEATGSAAH AAPAAELPSL LPDESAPEEF
FPGTQQEQIR VRAELLDNLV NHAGEVAIYR SRLEQQVSGY RFNLVELDQT VQRLRSQLRM
LEIETEAQII ARYQHEHREA GMATFDPLEL DRFSQLQQYS RALAESVSDL VSIQSMLDEL
TRQAETLLIQ QSRVSSELQE GLLRTRMLPF DTMVPNLRRT LRQAAQEQGK SAQLHVEGAH
GEMDRNLLDR IKAPFEHMLR NAVAHGIESP DERRKAGKSA EGAVRIRVAR EATEVVVRVS
DDGRGLDREA IRQRAVERGL LSADAKPGDE QLLGLITQTG FSTVDKVTQL AGRGVGMDVV
ANEIKQLGGS LAIDSQQGKG TTFVLRLPFT LAVTQAILVR IGESNFAIPM TSVQGVARIN
PDELVRRMAG HDPSFEYNNE EYGIHDLAEL LGQPVPHFGD EEQLPLLLTR SGDLRAAIRI
DEVIGSREIV VKSVGPQVSS VPGILGATIM GDGSVLVILD LAPLVRHGIG RREQRLAEGL
DVVQMPAIED VRALPLVMVV DDSITMRKVT GRVLERHEYE VVTAKDGVDA LEKLAERVPD
LMLLDIEMPR MDGYELATHM KADPRLRQVP IIMITSRTGE KHRQRAFDIG VERYLGKPYQ
EAELLAQIGE MMEQRAMEAG Q
//
