ID W0E2A8_MARPU Unreviewed; 700 AA.
AC W0E2A8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MARPU_07045 {ECO:0000313|EMBL:AHF03648.1};
OS Marichromatium purpuratum 984.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Marichromatium.
OX NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF03648.1, ECO:0000313|Proteomes:UP000005275};
RN [1] {ECO:0000313|EMBL:AHF03648.1, ECO:0000313|Proteomes:UP000005275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=984 {ECO:0000313|EMBL:AHF03648.1,
RC ECO:0000313|Proteomes:UP000005275};
RG DOE Joint Genome Institute;
RA Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007031; AHF03648.1; -; Genomic_DNA.
DR RefSeq; WP_005224628.1; NZ_CP007031.1.
DR AlphaFoldDB; W0E2A8; -.
DR STRING; 765910.MARPU_07045; -.
DR KEGG; mpur:MARPU_07045; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000005275; 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:SF1; 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:UP000005275};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 336..547
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 549..683
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 128..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 700 AA; 74455 MW; 1EF84AC84F2B4943 CRC64;
MPIDPNDEIL QDFLVEAGEL LEGLNEQLID LEQDPANRDL LNSVFRSFHT IKGGAGFLNL
NALVSVCHHA EDVFNLLRNG ERHVDAQLMD TVLRVLDVVN VMFGDLQSGK EPEPAAPELI
AELEQLASPA PPPASPEPPP APVEPPPAEP EAAPEPVVAT GASAPDDEIT EQEFEALLDA
LGGQPQSGAA PAEAAEPAVP ASSESIPIEA ATADEQPAED TDLITDEEFE NLLDQLHGKG
AFTAAPAPKA AAESAPSSPA PAPQPSTAAA PAKPAPKPDG ESSAAAAARA VKQVATPAET
SVRVDTNRLD EIMNLVGELV LVRNRLSMLR SQTEDDEVAK AINSLALVTA DLQAAVMKTR
MQPIKKVFSR FPRVVRDLSR SLGKEIDFQT YGEDTDLDKN LVEALADPLV HLIRNAVDHG
IEMPDVREAA GKSRRGRVIL GAAQEGDHIA LTIEDDGRGM DPQALRLKAV EKGLLEPPMA
ERLSDRDAFN LIFMAGFSTK EQISDVSGRG VGMDVVKTRI AQLNGSVEID SELGRGTLLQ
VKLPLTLAIL PALMVILDGR RFAIPLASVS EILDLDLSRS RFVDDQEAIV VRSHALPIYH
IGRWVRPGRE EGPRGEAHVV VVQVGQRKVG LVVDGLVGQE EVVIKPLGLG LRHVSGLAGA
TITGDGGIAL ILDVPELLKV MGRSEFGGRR EAADELVTGG
//
