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Database: UniProt
Entry: A0A1U7D0G9_9RHOB
LinkDB: A0A1U7D0G9_9RHOB
Original site: A0A1U7D0G9_9RHOB 
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};
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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
//
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