ID A0A845UXB4_9GAMM Unreviewed; 691 AA.
AC A0A845UXB4;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=G3I74_06275 {ECO:0000313|EMBL:NDY95328.1};
OS Wenzhouxiangella limi.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Chromatiales; Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=2707351 {ECO:0000313|EMBL:NDY95328.1, ECO:0000313|Proteomes:UP000484885};
RN [1] {ECO:0000313|EMBL:NDY95328.1, ECO:0000313|Proteomes:UP000484885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C33 {ECO:0000313|EMBL:NDY95328.1,
RC ECO:0000313|Proteomes:UP000484885};
RA Zhang X.-Y.;
RL Submitted (FEB-2020) 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 -!- 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:NDY95328.1}.
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DR EMBL; JAAGSC010000039; NDY95328.1; -; Genomic_DNA.
DR RefSeq; WP_164210722.1; NZ_JAAGSC010000039.1.
DR AlphaFoldDB; A0A845UXB4; -.
DR Proteomes; UP000484885; 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 FunFam; 2.30.30.40:FF:000048; Chemotaxis protein CheA, putative; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR FunFam; 1.20.120.160:FF:000008; Chemotaxis sensor histidine kinase CheA; 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; IPR051315; Bact_Chemotaxis_CheA.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000484885};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 2..106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 345..556
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 558..691
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 128..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 691 AA; 73422 MW; 5A42BCEBD132D3D9 CRC64;
MSFQLDDSIL EDFIAEAGEL VDGLGEELVQ LEQQPDDPAL LNSIFRAFHT VKGGAGFLNL
GSLVETCHSA ENVFDALRRG DLELNADIMD AVLQALDVVT DNMDSLRAGE ELAPPAPELI
QTLRGFVSGP QTEPATEPPP PAEHKPVEEK PAEPAALDPA DQAFEAMLAE AQGDGAGSEG
ADSDDSDLIT DDEFEALLDQ LEGKTPEATP APTAAPAAAA PAEPASDEIT DDEFEALLDD
LHGQGKAPTP QDGAEAAPAA APAEPPPPAA TAAPEKPAAP PEPAAAPAGN KADAAVARAV
KKAAAPQETS VRVDVSRLDA VMNLVGELVL VRNRLVNLGA SLHNEELQKA VANLDLVTGD
LQMGVMQTRM QPIRKVFSRF PRLTRDLART LNKEINLEMR GEETDLDKNL VEALADPLIH
LVRNSLDHGI EMPDEREAAG KPRAGTVELA AEQQGDHIVI TIGDDGAGID ADRLRDKAVK
KGQVSEEAAA KMTRQECFAL MFAPGLSTCD KVSEVSGRGV GMDVVKTRMA ELNGVIDIDS
EPGVGTTIQV RVPLTLAILP TLMVRLRQRI FAFPLTHVVE VFFLDRSRVR RVEGREVIMV
RGKPLPLVFL HRHLLRGVSE PEGVGYVVVL QIGNEKMGFV TDDVLGQEEV VIKPLGALLH
GIRGFAGATI TGDGKIALII DVNGLLRSVG G
//
