ID   CHED_VIBC3              Reviewed;         233 AA.
AC   A5F1A0; C3M728;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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};
GN   OrderedLocusNames=VC0395_0153, VC395_A1111;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ18634.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5F1A0; -.
DR   SMR; A5F1A0; -.
DR   STRING; 345073.VC395_A1111; -.
DR   PRIDE; A5F1A0; -.
DR   EnsemblBacteria; ABQ18634; ABQ18634; VC0395_0153.
DR   KEGG; vco:VC0395_0153; -.
DR   KEGG; vcr:VC395_A1111; -.
DR   PATRIC; fig|345073.21.peg.3834; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_0_6; -.
DR   OMA; VGMADLN; -.
DR   Proteomes; UP000000249; 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.
FT   CHAIN           1..233
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_1000073518"
SQ   SEQUENCE   233 AA;  26634 MW;  4DEDB36E957A4373 CRC64;
     MLVVAVRFSI IWDILFMSDS KLATKRKLKQ EEAKGQYYRF NHPSDHRHWV KVMPGGVYAT
     SDQEIIHTGL GSCVSACAWD IEMKVGGMNH FLLPFNNQFE SQHWHPQALL SDSSRYGCYA
     MEVLINRLLS MGAERERLKF KLFGGAHLMG YQSLVGEKNV EFVLEYAKRE KLNVVAQDLG
     GAQPRKLLFD PQAGQAWVKR IGFSSAHAIK QDEELYQHSI DKQIPSDDVE LFQ