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Database: UniProt/TrEMBL
Entry: E8TSU4_ALIDB
LinkDB: E8TSU4_ALIDB
Original site: E8TSU4_ALIDB 
ID   E8TSU4_ALIDB            Unreviewed;       245 AA.
AC   E8TSU4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   01-MAY-2013, entry version 14.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD;
DE            EC=3.5.1.44;
GN   Name=cheD; OrderedLocusNames=Alide_3837;
OS   Alicycliphilus denitrificans (strain JCM 14587 / BC).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Alicycliphilus.
OX   NCBI_TaxID=596153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14587 / BC;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Daligault H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Oosterkamp M.J.,
RA   Veuskens T., Weelink S.A., Plugge C.M., Stams A.J.M., Woyke T.;
RT   "Complete sequence of chromosome of Alicycliphilus denitrificans BC.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC       methyl-accepting chemotaxis receptors (MCPs), playing an important
CC       role in chemotaxis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein L-glutamine + H(2)O = protein L-
CC       glutamate + NH(3).
CC   -!- SIMILARITY: Belongs to the CheD family.
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DR   EMBL; CP002449; ADV01545.1; -; Genomic_DNA.
DR   RefSeq; YP_004128432.1; NC_014910.1.
DR   EnsemblBacteria; ADV01545; ADV01545; Alide_3837.
DR   GeneID; 10105918; -.
DR   KEGG; adn:Alide_3837; -.
DR   PATRIC; 45146588; VBIAliDen149934_3946.
DR   HOGENOM; HOG000273194; -.
DR   KO; K03411; -.
DR   BioCyc; ADEN596153:GHGY-3987-MONOMER; -.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:HAMAP.
DR   GO; GO:0006935; P:chemotaxis; IEA:HAMAP.
DR   HAMAP; MF_01440; CheD; 1; -.
DR   InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD.
DR   Pfam; PF03975; CheD; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Complete proteome; Hydrolase.
SQ   SEQUENCE   245 AA;  26688 MW;  274D1917756299DF CRC64;
     MSVPTRPDAR PAGAPGGLPE RRHVPRIAPL GVDVRAPDAA PEVSLQELKA RARKPGEASF
     FFFDHHFQHN AVKVLPGEFF VARERIAIMT VLGSCIAACL WDSRAGVGGM NHFMLPEGGS
     ADTSGRYGSY AMELLINEMM KLGARRETLQ AKIFGGGQVM HNFTTMNVGE RNTRFVQNYL
     ATERIPVVSE DVLDIYPRKV VFFPATGKAM VKRLAHAHPE SLAQEVRGNA ATVARTTSGG
     SVDLF
//
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