ID A0A0P1G5G0_9RHOB Unreviewed; 727 AA.
AC A0A0P1G5G0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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:CUH77026.1};
GN ORFNames=TRM7557_01173 {ECO:0000313|EMBL:CUH77026.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH77026.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH77026.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH77026.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-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};
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DR EMBL; CYSD01000017; CUH77026.1; -; Genomic_DNA.
DR RefSeq; WP_058289290.1; NZ_JAQIPA010000018.1.
DR AlphaFoldDB; A0A0P1G5G0; -.
DR STRING; 928856.SAMN04488049_1198; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000052022; 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:UP000052022};
KW Transferase {ECO:0000313|EMBL:CUH77026.1}.
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 317..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 577..712
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 264..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 727 AA; 77497 MW; 179F6BA885EAB67D CRC64;
MSGSIQDTFF EECEELLEAM DEGLTAVEGG DHDPEIVNAV FRAVHSIKGG AGAFGLDELV
GFAHKFETVF DEVRSNKVQL DTKLIQLLLR CSDHLADLVA VARDGGSTDE EHHDTLIAGL
EEYLDEEEEE LTFEPMGLGG PAAPPPLAIE SEKNYTIRFQ PLKEMFGTGN EPFFLFQALS
ELGDLKVVLD ESELPGFDSM DMAESYLAWD LELTSSEPQS RVEAVFEFVE GLCELSIASD
KDDEEEAAAL EALNAAFGAD AGPLGSGLPE VTPPAAAPAE APETDTSGPF EAPAPAEEVK
VAEAEPVEQA EAASPEAAKK EQRGPKPTLR VELERVDRLI NAVGELIINH SMLAQQIANL
NAGDMRDVET ELEGFKNLAR DIQEGVMAIR AQPVKPLFQR MARIVREASS ATEKQAKLIN
EGENTEVDKT VIERLSDPLT HILRNAVDHG LEKPEDREAA GKSRVGEIRL SASHRSGSVC
IEIKDDGAGI NRPKVKQIAI EKGLIPENAE LTDSEIDNLL FLPGFSTAKE VSNLSGRGVG
MDVVKNAVTG LGGRISITST PGKGSTFTII LPLTLAVMDG MVVSVGGQTM VVPITSIVET
MRGSDDMINS LGADGTLLSI RGNFVPICDV AGALGLMKPD DQPPGVYLLV ETETGQRSAL
AVDDIHDQRQ VVIKSLDGVC GNIPGVAAAT ILGDGKIAMI LDPESIISAG GTAGFDTERR
MSNAIAS
//