ID   CHED_STRM5              Reviewed;         198 AA.
AC   B4SHX1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=Smal_1844;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF51548.1; -; Genomic_DNA.
DR   RefSeq; WP_008264676.1; NC_011071.1.
DR   AlphaFoldDB; B4SHX1; -.
DR   SMR; B4SHX1; -.
DR   STRING; 391008.Smal_1844; -.
DR   EnsemblBacteria; ACF51548; ACF51548; Smal_1844.
DR   KEGG; smt:Smal_1844; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_0_6; -.
DR   OMA; VGMADLN; -.
DR   OrthoDB; 1863047at2; -.
DR   BioCyc; SMAL391008:SMAL_RS09440-MON; -.
DR   Proteomes; UP000001867; 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..198
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_1000145895"
SQ   SEQUENCE   198 AA;  21648 MW;  0508D570842DBEA9 CRC64;
     MNASLRTDDV MRYQDARFKT IAAKLLPTQY LVVDDTTALT TTLGSCVAAC LRDPVLKIGG
     MNHFLLPEGN AGDGAPARYG SYAMELLIND MLKRGAHRKR IEAKVFGGAN VLKGFTSNPV
     GTRNAEFVRQ YLQAEHIPII AEDLCGIHPR KIWFFADTGR VVVQRLPHAH EAEVAATESA
     VRARLSKAPV TGGVELFE