ID   CHED2_RUEST             Reviewed;         179 AA.
AC   Q1GM98;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD 2 {ECO:0000255|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   Name=cheD2 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   OrderedLocusNames=TM1040_3244;
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; ABF62218.1; -; Genomic_DNA.
DR   RefSeq; WP_011536862.1; NC_008043.1.
DR   AlphaFoldDB; Q1GM98; -.
DR   SMR; Q1GM98; -.
DR   EnsemblBacteria; ABF62218; ABF62218; TM1040_3244.
DR   KEGG; sit:TM1040_3244; -.
DR   HOGENOM; CLU_087854_2_0_5; -.
DR   OMA; RISINCD; -.
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..179
FT                   /note="Probable chemoreceptor glutamine deamidase CheD 2"
FT                   /id="PRO_0000251067"
SQ   SEQUENCE   179 AA;  19173 MW;  02564ECDBA083940 CRC64;
     MDKVEVSELH VRIGQVKIGS PGQVLTAILG SCVGIGFFFP QRQIYGLAHC LLSQSSSQPV
     ASSAAQTGRT REDGQLVGNG RHVDKAIESL LKMMDIQDEE RRQLRVVLAG GANMSMPFDT
     PPSQLVGSVN AKFARQAIRS AGLRLLGDDL GGLNGRRISI NCDSGEYDIQ QIPRLGGTV