ID   CHED_BURMA              Reviewed;         234 AA.
AC   Q62G11;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BMA2855;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU48334.1; -; Genomic_DNA.
DR   RefSeq; WP_004198646.1; NC_006348.1.
DR   RefSeq; YP_104366.1; NC_006348.1.
DR   AlphaFoldDB; Q62G11; -.
DR   SMR; Q62G11; -.
DR   STRING; 243160.BMA2855; -.
DR   EnsemblBacteria; AAU48334; AAU48334; BMA2855.
DR   GeneID; 56593993; -.
DR   KEGG; bma:BMA2855; -.
DR   PATRIC; fig|243160.12.peg.2926; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_0_4; -.
DR   OMA; VGMADLN; -.
DR   Proteomes; UP000006693; Chromosome 1.
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..234
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_0000251013"
SQ   SEQUENCE   234 AA;  25682 MW;  8BAA17C949315C22 CRC64;
     MSGLPIATNL YFDAHFHRHG VKLLPNEFYT TREDMVLVTV LGSCVAACLH DPIGRIGGMN
     HFMLPDDGAD PSAAASESMR YGAYAMEVLI NELIKAGGRR ERFEAKVFGG AAVLAGMTTI
     NIGDRNADFV RRYLALERIR ITAEDLQGVH PRKVAFMPHT GQAMVKKLRV QAPDVAAREA
     ALAREAVDPH GERAPRVRPR VELFGTPAPK AQAKPRIELF GMRATQPATR KQEA