ID   CHED_CERS4              Reviewed;         199 AA.
AC   Q3J3N4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=RHOS4_10320;
GN   ORFNames=RSP_2439;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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; CP000143; ABA78600.1; -; Genomic_DNA.
DR   RefSeq; WP_011337491.1; NZ_AKVW01000001.1.
DR   RefSeq; YP_352501.1; NC_007493.2.
DR   AlphaFoldDB; Q3J3N4; -.
DR   SMR; Q3J3N4; -.
DR   STRING; 272943.RSP_2439; -.
DR   EnsemblBacteria; ABA78600; ABA78600; RSP_2439.
DR   KEGG; rsp:RSP_2439; -.
DR   PATRIC; fig|272943.9.peg.1358; -.
DR   eggNOG; COG1871; Bacteria.
DR   OMA; VGMADLN; -.
DR   PhylomeDB; Q3J3N4; -.
DR   Proteomes; UP000002703; 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; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_0000251059"
SQ   SEQUENCE   199 AA;  21592 MW;  68A00C125A02C4AC CRC64;
     MTRCDDSPSA SQISITHVTQ GSCVASSSPN EVYATILGSC ICTCMCDPVA GVGGMNHFLL
     PSADVEDAQH LRYGSHAMEL LINALLKLGA ARQRIEAKIF GGAMMTPQLG AIGQANAAFA
     RRYLKDEGIR CTAHSLGGNR ARRIRFWPKT GRVQQMFLGS EDVVPNEQPQ FRLQGGAGDV
     TFFDRHNNAE MPDPIKEPR