ID   CHED_BACVZ              Reviewed;         166 AA.
AC   A7Z4R7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Chemoreceptor glutamine deamidase CheD {ECO:0000255|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   Name=cheD {ECO:0000255|HAMAP-Rule:MF_01440}; OrderedLocusNames=RBAM_016300;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
CC   -!- FUNCTION: Deamidates glutamine residues to glutamate on methyl-
CC       accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is
CC       required for productive communication of the conformational signals of
CC       the chemoreceptors to the CheA kinase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC         Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01440};
CC   -!- SUBUNIT: Forms a complex with CheC. {ECO:0000255|HAMAP-Rule:MF_01440}.
CC   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01440}.
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DR   EMBL; CP000560; ABS73993.1; -; Genomic_DNA.
DR   RefSeq; WP_003154219.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4R7; -.
DR   SMR; A7Z4R7; -.
DR   STRING; 326423.RBAM_016300; -.
DR   PRIDE; A7Z4R7; -.
DR   EnsemblBacteria; ABS73993; ABS73993; RBAM_016300.
DR   GeneID; 66326364; -.
DR   KEGG; bay:RBAM_016300; -.
DR   HOGENOM; CLU_087854_2_0_9; -.
DR   OMA; VGMADLN; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   CDD; cd16352; CheD; 1.
DR   Gene3D; 3.30.1330.200; -; 1.
DR   HAMAP; MF_01440; CheD; 1.
DR   InterPro; IPR038592; CheD-like_sf.
DR   InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD.
DR   InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR   PANTHER; PTHR35147; PTHR35147; 1.
DR   Pfam; PF03975; CheD; 1.
DR   SUPFAM; SSF64438; SSF64438; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Hydrolase.
FT   CHAIN           1..166
FT                   /note="Chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_1000068542"
SQ   SEQUENCE   166 AA;  17952 MW;  5F3068FB292BAB13 CRC64;
     MSRAEAAVVK VGIADVQVAR YPDKIRTSGL GSCVGLVLYD KDKQTAGLVH VMLPDSGLSK
     TAELNRAKYA DTAVKMTIDM LLKAGCRKFA LKAKLAGGAE MFKFKMTNDL MKIGPRNVAA
     IKEQLSLYNI PVISEDTGGS SGRTIEFEPK SCMLHIRTVK QGETTI