ID D0YZ71_PHODD Unreviewed; 767 AA.
AC D0YZ71;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Phosphorelay protein LuxU {ECO:0000256|ARBA:ARBA00017260};
GN ORFNames=VDA_002584 {ECO:0000313|EMBL:EEZ41552.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ41552.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ41552.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ41552.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) 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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR EMBL; ADBS01000001; EEZ41552.1; -; Genomic_DNA.
DR RefSeq; WP_005300396.1; NZ_ADBS01000001.1.
DR AlphaFoldDB; D0YZ71; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR Proteomes; UP000003579; 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: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:UP000003579};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 416..627
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 629..765
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 191..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 767 AA; 83076 MW; 1BBE7EF59E7D95AF CRC64;
MSFDLDEDIL QDFLIEAGEI LELLSEQLVE LERSPENSEL LNAIFRGFHT VKGGAGFLSL
TELVDVCHGA ENVFDLLRTG KRHVTSELMD VILQALDTIN VMFALVQDRE PLEQADPSLL
AALHRFSQPG DASVAEPIVV TPVVEPEPEI VVVDVPASAS SHQEDQPVTS GSSVDDITQD
EFERLLDELH GVGKGPSVNE GSSATQSSAP VSNSASTSTQ PSDVVRLHIE SDSNDITDDE
FERLLDELHG SGKGPSSHED NVAGTESSIV ADSANEQTAA EVTSGDEELM SDDEFERLLD
QLHGIGKGPS AQELEAATCS VAEMNDQKDE PAPVSQPVSS SERSESQPTP VVAPIRTAEP
VAVRETAVKE KAISKPTAET TVRVDTSTLD TIMNMVGELV LVRNRLVSLG LNSNDEEMSK
AVANLDVVTA DLQGAVMKTR MQPIKKVFGR FPRVVRDLAR HLKKDIVLEM QGEETDLDKN
LVEALADPLV HLVRNSVDHG IEMPEVRERI GKPRTGTVLL SASQEGDHIL LTIEDDGNGM
DANKLRAIAV ERGIMDSDAA SRLTDNEAYN LIFAPGFSTK KEISDISGRG VGMDVVKTAI
SQLNGSIHID SAMGKGTRIE IKVPLTLAIL PTLMVGVADQ PFALPLASVN EIFHLDLRKT
NIVDGQLTTI VRDKAVPLFY LQDWLAPRYY TEHKDRDHGH VVIVQIGHQR IGFVVDTLVG
QEEVVIKPLD ELLQGTPGMA GATITSDGHI ALILDVPNLL KHYAGRK
//