ID   CHED2_ALBFT             Reviewed;         173 AA.
AC   Q220A0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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}; OrderedLocusNames=Rfer_0905;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-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; CP000267; ABD68653.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q220A0; -.
DR   SMR; Q220A0; -.
DR   STRING; 338969.Rfer_0905; -.
DR   EnsemblBacteria; ABD68653; ABD68653; Rfer_0905.
DR   KEGG; rfr:Rfer_0905; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_1_1_4; -.
DR   OMA; ITLWHPA; -.
DR   Proteomes; UP000008332; 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; Reference proteome.
FT   CHAIN           1..173
FT                   /note="Probable chemoreceptor glutamine deamidase CheD 2"
FT                   /id="PRO_0000251061"
SQ   SEQUENCE   173 AA;  18822 MW;  28BBF94BF5B13FD5 CRC64;
     MSRKKKPIDI FLQPGEYFVA DAGYQIRTML GSCVSITLWH PATRQGAMSH FLLPTRGASK
     PKQTLDARYG DEALKLMLIE LQRLGIPSAQ CQGKIFGGGN MFPGNLRSGA LNVGQRNGEA
     ALTLLREHGI PVMSESLFGI GHRQIVFDVS NGDVWSHQVM PIGTDSGDKG DLL