ID A0A0C9NFC7_SPHPI Unreviewed; 656 AA.
AC A0A0C9NFC7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:GAN13453.1};
GN ORFNames=SP6_18_00180 {ECO:0000313|EMBL:GAN13453.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN13453.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN13453.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN13453.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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:GAN13453.1}.
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DR EMBL; BBJS01000018; GAN13453.1; -; Genomic_DNA.
DR RefSeq; WP_007403742.1; NZ_BBJS01000018.1.
DR AlphaFoldDB; A0A0C9NFC7; -.
DR GeneID; 78527114; -.
DR Proteomes; UP000032025; 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}.
FT DOMAIN 3..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 309..513
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 515..647
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 656 AA; 70102 MW; A1ABB3035EB305F2 CRC64;
MSGPGSGEDP TAAFRIEAGE LLEQVEQGLL DLGHRLDDMG LVNAVFRGLH TLKGSGAMFG
FDALAAFTHH CESAFDRVRK GDVRATPELV SVILSAGDHM RALVEGDAPA AEGQVILARL
AAAVDAAAGG GASASAVAAK RGWTLSFRLP PDAMANGTNP LALLDELREL GEATIVARID
DVPTLDELNP SHCMIGWDCT LIGDISKDAI EDVFLFVMDD MEITITPLTV EDDAPVAAVA
VDDVAQTTEP VAANDTGARA TTSRVQGENV RVPAERLDEL MDRVGELVIA QSRLSQLAAH
GHDLSLRSVS EEIERLTGEM RDTMMILRMV PVSTLFGRFR RLIHDLAIET GKAIELVTEG
ESTEVDKTVI ERLFDPLVHI IRNSCDHGLE MAEDRQAAGK PAAGRIRLSA HQVGGEVLIT
ITDDGRGIDR ERVRAKAEAN GLIQPGQVLT DDELLGLIFH PGFSTAAQVT NLSGRGVGMD
VVKRTIESLR GSIDVKSVAG QGSTITLRIP LTLAIIEGLL VRVGEGRYVI PLSAVEECLE
LSLEEDLRSR GRSVITLRET LVPFLRLREM FATGTKPDPF QKIVVVSTGR ERVGLVVDQI
IGNHQTVIKS LSAFHRGAAS FSGATILGDG SVALILDVAQ LVAMAQPQEE MLRAAG
//
