ID   CHED1_RUEST             Reviewed;         187 AA.
AC   Q1GMD1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD 1 {ECO:0000255|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   Name=cheD1 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   OrderedLocusNames=TM1040_3211;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OG   Plasmid megaplasmid TM1040.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of megaplasmid of Silicibacter sp. TM1040.";
RL   Submitted (MAY-2006) 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; CP000376; ABF62185.1; -; Genomic_DNA.
DR   RefSeq; WP_011536829.1; NC_008043.1.
DR   AlphaFoldDB; Q1GMD1; -.
DR   SMR; Q1GMD1; -.
DR   EnsemblBacteria; ABF62185; ABF62185; TM1040_3211.
DR   KEGG; sit:TM1040_3211; -.
DR   HOGENOM; CLU_087854_0_1_5; -.
DR   OMA; RIGGMCH; -.
DR   OrthoDB; 1863047at2; -.
DR   Proteomes; UP000000636; Plasmid megaplasmid TM1040.
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..187
FT                   /note="Probable chemoreceptor glutamine deamidase CheD 1"
FT                   /id="PRO_0000251066"
SQ   SEQUENCE   187 AA;  19591 MW;  7E0C3FB62CF50A35 CRC64;
     MSNVFQNTST VTVLQGDYKV TTDPKVVFST VLGSCIAACI YDEQVGVGGM NHFLLASSAG
     SGGVSARYGV HAMELLINGI MKKGALRSNL KAKVFGGAKM SANLSDIGAN NADFVQRFLR
     DEGIPVISSS VGGTSARRVR FHACSGAAQQ THVADDRRLG EEERAAVART QAAPARKPAA
     ADNVTLF