ID A0A2R8AVL6_9RHOB Unreviewed; 404 AA.
AC A0A2R8AVL6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA_3 {ECO:0000313|EMBL:SPF80076.1};
GN ORFNames=PRI8871_01878 {ECO:0000313|EMBL:SPF80076.1};
OS Pseudoprimorskyibacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoprimorskyibacter.
OX NCBI_TaxID=1695997 {ECO:0000313|EMBL:SPF80076.1, ECO:0000313|Proteomes:UP000244904};
RN [1] {ECO:0000313|Proteomes:UP000244904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8871 {ECO:0000313|Proteomes:UP000244904};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAR-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OMOJ01000003; SPF80076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AVL6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000244904; 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 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000244904};
KW Transferase {ECO:0000313|EMBL:SPF80076.1}.
FT DOMAIN 60..264
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 266..404
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
SQ SEQUENCE 404 AA; 43868 MW; 0A618E6D7823985B CRC64;
MAAEVETTSE KTTGGALLRV SSDKIGRLMD LVGELSLSVS ETINSPELAD LDLMGFEAAA
HRLSMIVREV QDAATELRLV PVGEVFRRLK RMIRELERET GKKIELVIKG DETAIDKLVA
DRLYDPLLHV VRNAADHGLE ATTADRVAVG KSESGKITLA AAQVGSEVRI QVIDDGRGLN
RDRILKKARE RGLFGPEEEP ENSAVWKVIF EPGFSTAEAV TTLSGRGVGM DVLNQTMKDL
RGRIAVDSNP GEGTAVSLHI PVSLAFLDSI LLRLGEKLFT VPVDDIQEIV KPGGSDTVSI
SADHDTEMLK LRGVFVPVCR LERFYRGMRQ ELKPLSQMVA IIFNTANGAI AVPVDEVLDR
QQVVMKPLTG ALSSVRASWG CALLPSGEVA IVLDCERLAL ESAR
//
