ID A0A0M3ARA0_9SPHN Unreviewed; 789 AA.
AC A0A0M3ARA0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-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 ORFNames=YP76_11070 {ECO:0000313|EMBL:KKW92438.1};
OS Sphingobium chungbukense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW92438.1, ECO:0000313|Proteomes:UP000033874};
RN [1] {ECO:0000313|EMBL:KKW92438.1, ECO:0000313|Proteomes:UP000033874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW92438.1,
RC ECO:0000313|Proteomes:UP000033874};
RA Kim Y.-C., Chae J.-C.;
RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT chungbukense DJ77.";
RL Submitted (APR-2015) 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:KKW92438.1}.
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DR EMBL; LBIC01000004; KKW92438.1; -; Genomic_DNA.
DR RefSeq; WP_046763644.1; NZ_LBIC01000004.1.
DR AlphaFoldDB; A0A0M3ARA0; -.
DR STRING; 56193.YP76_11070; -.
DR PATRIC; fig|56193.3.peg.2299; -.
DR Proteomes; UP000033874; 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; 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 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:SF1; 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 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 148..399
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 401..537
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 789 AA; 85361 MW; C24BAC0408A4D791 CRC64;
MDELLQEFIS ETQETLEALA GEVVAWEADP ADRDRLDAIF RFFHTVKGSC GFLNLPRFER
LSHAAEDVLA EIRADRRSAD PATVSAVLGI MDRIAELAEA VSLGTALPHE NDDYLIAALS
EKEEDEAVLP EAESAPVAVA RQQGNGQAAP RTIRLPLSLI DQLMNGVSDM VLARNELSRK
LRERTGDPEL ESAFERLSTC VADMRDAISK TRMQRVDRLF TAIPRMVRDL GRELGKRIDL
LLEGGDVEMD REMVEMVVDP LTHIVRNSID HGIETPEKRR ALGKSEAGRL KLEARQSGNQ
IVIEISDDGQ GIDTGRLVGK AIAAGRLTPE SAARMSEAEK LDLIFHPGLS TADQVTAISG
RGVGMDVVRA NVERIGGVIS LDNRPGRGLT IMLRVPLTLT IIPGLIVRAG GLHFAIPRAA
VVEILHDNNE TLHIAEVGGA KIATIRSIRH SMIDLEDVLG MEKPAQTGPR AVMVVRSATG
VPFAMGVSAV DNHEELVIRP ASPLVMATGV YAGMTLPDNG KPMLLLDAAG LANAARLPNI
LDDRAAREAE EAVDVQGVEM VPALRFEEYS GERRLLKLSL IERVEDVDAH LFGRSGGRAY
VRLDDRLVPV ANGHHSFVGE KVAALRLRDG TRDVCYPVAA VLDIVDMPAV PDMIAMHGTL
SGVVVIDGEH LEVVNPFALF AALPDEPIRE KGRGRCLLAD SEDGWTREIL APLLRQAGHE
VVLGLPADAP VDPQDVVLFS GADLSQASEL LGCRVVHLRA SPRPSSPQDG SIYRYDQDAL
MAALAGSRG
//
