ID A0A1U7D0G9_9RHOB Unreviewed; 713 AA.
AC A0A1U7D0G9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Ga0080559_TMP848 {ECO:0000313|EMBL:APX21644.1};
OS Salipiger profundus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX21644.1, ECO:0000313|Proteomes:UP000186559};
RN [1] {ECO:0000313|EMBL:APX21644.1, ECO:0000313|Proteomes:UP000186559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2016 {ECO:0000313|EMBL:APX21644.1,
RC ECO:0000313|Proteomes:UP000186559};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
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 ---------------------------------------------------------------------------
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; CP014796; APX21644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7D0G9; -.
DR STRING; 1229727.Ga0080559_TMP848; -.
DR KEGG; tpro:Ga0080559_TMP848; -.
DR Proteomes; UP000186559; Chromosome.
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 Kinase {ECO:0000313|EMBL:APX21644.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000186559};
KW Transferase {ECO:0000313|EMBL:APX21644.1}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 300..558
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 560..696
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 266..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 713 AA; 76992 MW; B2D724077CCA3A05 CRC64;
MTMSRNAIRD TFFEECEELL EALVEGLSSM EADAGNMEVV NAVFRAVHSI KGGAGAFALD
RLVNFAHTFE TVMDKVRSQE LTVDEELMLL FHRSGDQLAD LVEAARDERE PNAESEAAIL
KELEAHLGEA DKEEDFAFDA VTLDFDATPA PLELAEDTPE LRRFDIRFKP KPALYANGHE
PLLLFDALAE LGTLSVTANI ADLPDFDAFD PNDAVIDWHL TLDTAEDETV LHEIFEFVDA
LCELDISVNE DPQPALEVSA LAEAPAPPTV TSLENEPIEA PAPLRQSEDR PPAPEPKPSV
ARDEPRGPKP TLRVDLDRVD RLINTVGELI INQAMISQRI EELELPAVAH LTNELEAYKL
LARDIQEGVM AIRAQPVKPL FQRMSRIVRE ASEATGKKAK LVTVGDSTEV DKTVIERLAD
PLTHMVRNAV DHGLELPERR EEAGKDPVGS IRLSASHRSG SVFIEIADDG AGLNRARVLE
KAIEKGLIAP DAELSEQETD NLLFLPGFST ASEISNLSGR GVGMDVVKNA VSGLGGRVSI
TSTAGAGTTF TIVLPLTLAV MDGFVISIAD QTMVIPIASI IETIRPNRKD LHHIGTGGEV
ISVRGAYVPI VDVARNLGLS HGADDIGSGV LLLVSTESHG LTALRVGAIH DQRQVVIKSL
ESNYGAIPGV SAATILGDGK IALILDPDEL VKLNPAAPFL PPASTPRMEL RHA
//