ID A0A2A8HV18_9SPHN Unreviewed; 726 AA.
AC A0A2A8HV18;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B2G71_10915 {ECO:0000313|EMBL:PEQ12794.1};
OS Novosphingobium sp. PC22D.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1962403 {ECO:0000313|EMBL:PEQ12794.1, ECO:0000313|Proteomes:UP000220675};
RN [1] {ECO:0000313|EMBL:PEQ12794.1, ECO:0000313|Proteomes:UP000220675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC22D {ECO:0000313|EMBL:PEQ12794.1,
RC ECO:0000313|Proteomes:UP000220675};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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:PEQ12794.1}.
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DR EMBL; MWMO01000005; PEQ12794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8HV18; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000220675; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000220675}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 381..581
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 583..719
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 126..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..323
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 726 AA; 75108 MW; 20C92FC1A30C5E9D CRC64;
MTPEEIQQIF FVECEESLAA AEAGLAACQT GTQDGDTING VFRAVHSIKG GAGAFGYTAL
QAYTHTFETL LSDVREGTVD LGDALIGLLL RALDTLSDHV EAAREGGDAP ADAALIAEME
AAQAGGSGAV PATAEPEPAV TAAPSEPAGQ SDGEGGDDLD LDLDSLLDDI SGGFSAPQAE
AEAEAEKPWQ VHVRPHAGAM RNGSEPLLML RDLADLGGTC VRCDVGAVPA LDGFDPGQGY
LGWTFAMPAS VEADTVRDIF DFVGKDCTIA IGEDEGIPPV EIEPAAAPAP APAPVAKPGV
EAAQKPAEPA AQKPAEPAAP AAAAAPNAPP AAVAAGQSIR IDLFKLDRLI DLVGELVIAQ
AMLVQRLDGA GITATEELGL LENLTRDIQE SAMSIRAQPI SSVFSRVPRI LRDLASTTGK
HVKLEVIGES TELDKTVIER LGEPLTHLIR NAVDHGIESA EDRIAAGKNP EGTLTLSAEH
RSGRILISIA DDGAGINRER VLAKAIEKGI VSAENQLTAE EIDNLIFAPG FSTAQTISSV
SGRGVGMDVV RQNVKDLGGR ITIDSTPGEG TTFILTLPLT LAISDGMIVN VGEQTLVVPL
AHVLESLRPA EGDVKGLGSS RHMLNVRGKF IPVLSLREAL GSPSGATSPE EGVLIVVDTE
AAGQAALLVD DIQDQRQFVI KSLSTNYRSV DGVAGATILG DGRVALIVDV DGLVACALPA
HERQAA
//
