ID A0A176FVN0_9RHOB Unreviewed; 645 AA.
AC A0A176FVN0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A3731_27950 {ECO:0000313|EMBL:KZY48415.1};
OS Roseovarius sp. HI0049.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1822235 {ECO:0000313|EMBL:KZY48415.1, ECO:0000313|Proteomes:UP000077043};
RN [1] {ECO:0000313|EMBL:KZY48415.1, ECO:0000313|Proteomes:UP000077043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0049 {ECO:0000313|EMBL:KZY48415.1,
RC ECO:0000313|Proteomes:UP000077043};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00110}.
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:KZY48415.1}.
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DR EMBL; LWFA01000130; KZY48415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176FVN0; -.
DR Proteomes; UP000077043; 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 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;
FT DOMAIN 1..56
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 295..495
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 497..633
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 197..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZY48415.1"
SQ SEQUENCE 645 AA; 68142 MW; B00C65D4C7D338CE CRC64;
IKGGAGAFGF TDLVTFAHQF ETALDHVRSG KCDADEELLD LFRQCGDHLA DLVAAARCEG
DAPPRGEGLL DRLAEATGTG DSGAEEILPD FEPVTLDLGG NASDDRALTL RFAAEPGLFT
SGNEPLILFR ALAGLGTLEV EANLSDVPPL DALDPTACRI DWSLRLVTAA SDDDIREVFE
FVEGLCRLEI EPDAIADPAP EALPDGPLPS LSDLIGGGDD SASTDPAATG PDPSAARPEA
SAPRPGGTIR VDLEKIDKLI NLVGELVIKE AMLSQSIADL PGQAESDLSA SLESLKQLAG
EIQEGVMAVR AQPVKPMFQR MARIVREAGA ATGKRVKFVT NGEFTEVDKT VIERLVDPLT
HMIRNAIDHG LETGDQREAV GKPREGTVTI SAAHRSGRVM IDVADDGGGI NREKVRALAI
ERGLISGAES LSASEIDNLL FLPGFSSKDE VSELSGRGVG LDVVRSEIQT LGGRVAIHSE
PGEGTVFSIS LPLTLAVLEG MVIRVANQTM VVPISAMHET LQPRSAAIHP IGAGGWVLRN
RTGLVPVIDL GHFFGFRGPV TEIDSHVLLL IESDASQYFA LIVDDIQEQR QVVIKSLETN
YQQVQGVAAA TILGDGRIAL IIDPDNITRG SVALGGAHSS IQMAV
//
