ID A0A1Q9GN17_9GAMM Unreviewed; 778 AA.
AC A0A1Q9GN17;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BIT28_18745 {ECO:0000313|EMBL:OLQ76057.1};
OS Photobacterium proteolyticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1903952 {ECO:0000313|EMBL:OLQ76057.1, ECO:0000313|Proteomes:UP000186905};
RN [1] {ECO:0000313|EMBL:OLQ76057.1, ECO:0000313|Proteomes:UP000186905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13-12 {ECO:0000313|EMBL:OLQ76057.1,
RC ECO:0000313|Proteomes:UP000186905};
RA Li Y.;
RT "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (SEP-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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLQ76057.1}.
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DR EMBL; MJIL01000069; OLQ76057.1; -; Genomic_DNA.
DR RefSeq; WP_075763981.1; NZ_MJIL01000069.1.
DR AlphaFoldDB; A0A1Q9GN17; -.
DR STRING; 1903952.BIT28_18745; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000186905; 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:UP000186905};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 429..640
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..777
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 130..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
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 778 AA; 82020 MW; B0E68EAA5EA8B318 CRC64;
MSFDLDEDIL QDFLIEAGEI LELLSEQLVE LERSPEDSEL LNAIFRGFHT VKGGAGFLSL
TELVDACHGA ENIFDLLRTG KRSVTPELMD VILEALDTIN EMFGLVQERE PLVPAEQSLL
DALHRYSQPP TAEELAPAAA APVSEPEPVV VPEPVAPSPV VEPAAAQPAA PSSAIAGDTV
DDMTQDEFDR LLDELHGAGS GPSASSAAPT PASAPAPQAG NAAVVDQIQS ESGDITDDEF
ERLLDELHGA GKGPGNTDSV VVATPVPATP APAAPVAAST VPSDTGASSG DDDLMTDDEF
ERLLDELHGS GKGPSAEELE MATCPVADML ADVSKPASAE VPVAPVAPAA ATAAPAASAP
VASSPAPASK PVAERKPKAV AAAKDKGKPA AEATVRVDTS TLDTIMNMVG ELVLVRNRLV
SLGLNTNDEE MSKAVSNLDV VTADLQGAVM KTRMQPIKKV FGRFPRVVRD LARSLKKEIV
LEMRGEETDL DKNLVEALAD PLVHLVRNSV DHGIEMPDAR EKAGKPRLGT VLLSASQEGD
HILLTIEDDG GGMDPDKLRN IAVDRGVMDA DAASRLTDSE CYNLIFAPGF STKKEISDIS
GRGVGMDVVK TGISQLNGSI SIDSALGKGT RIDIKVPLTL AILPTLMVGV AEQPFALPLA
SVNEIFHLDL RKTNNVDGQL TIIVRDKAIP LFYLQDWLSA VGLPQRERDH GHVVIVQIGH
QRIGFVVDTL IGQEEVVIKP LDELLQGTPG MAGATITSDG HIALILDVPN LLKHYAGR
//
