ID   CHED_CUPMC              Reviewed;         220 AA.
AC   Q1LH12;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Probable 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=Rmet_3692;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid megaplasmid.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC       methyl-accepting chemotaxis receptors (MCPs), playing an important role
CC       in chemotaxis. {ECO:0000255|HAMAP-Rule:MF_01440}.
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   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01440}.
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DR   EMBL; CP000353; ABF10564.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1LH12; -.
DR   SMR; Q1LH12; -.
DR   STRING; 266264.Rmet_3692; -.
DR   EnsemblBacteria; ABF10564; ABF10564; Rmet_3692.
DR   KEGG; rme:Rmet_3692; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_0_4; -.
DR   OMA; VGMADLN; -.
DR   Proteomes; UP000002429; Plasmid megaplasmid CH34.
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; Plasmid; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_0000251054"
SQ   SEQUENCE   220 AA;  24534 MW;  2856CD64569503FC CRC64;
     MMRGTPQMPE AIATRKYFDR EFDRQAIKLL PNEYYVTAED VVLTTVLGSC VSACIRDEVA
     GVGGMNHFML PDDENAGADR MLSTSMRYGC YALEVLINEL LKMGARRERL EAKVFGGGAV
     LANMTTLNIG DRNADFVLKY LRTEEVRVAA QDLRGPHARR VSYFPRTGLA LVRRLTRQDD
     TVGIEREERA LARALSTSTK APARGAVELF TRQTTARIPT