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Database: UniProt
Entry: A0A1V2YL70_9FIRM
LinkDB: A0A1V2YL70_9FIRM
Original site: A0A1V2YL70_9FIRM 
ID   A0A1V2YL70_9FIRM        Unreviewed;       161 AA.
AC   A0A1V2YL70;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   03-MAY-2023, entry version 18.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000256|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_01440};
GN   Name=cheD {ECO:0000256|HAMAP-Rule:MF_01440};
GN   ORFNames=BEN19_05920 {ECO:0000313|EMBL:OOB80236.1};
OS   Epulopiscium sp. Nuni2H_MBin003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Candidatus Epulonipiscium.
OX   NCBI_TaxID=1884657 {ECO:0000313|EMBL:OOB80236.1, ECO:0000313|Proteomes:UP000189211};
RN   [1] {ECO:0000313|EMBL:OOB80236.1, ECO:0000313|Proteomes:UP000189211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nuni2H_MBin003 {ECO:0000313|EMBL:OOB80236.1};
RA   Ngugi D.K., Miyake S., Stingl U.;
RL   Submitted (JUL-2016) 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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01440};
CC   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01440}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOB80236.1}.
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DR   EMBL; MDJN01000049; OOB80236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2YL70; -.
DR   STRING; 1884657.BEN19_05920; -.
DR   Proteomes; UP000189211; Unassembled WGS sequence.
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:SF1; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED; 1.
DR   PANTHER; PTHR35147; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR   Pfam; PF03975; CheD; 1.
DR   SUPFAM; SSF64438; CNF1/YfiH-like putative cysteine hydrolases; 1.
PE   3: Inferred from homology;
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW   Rule:MF_01440};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189211}.
SQ   SEQUENCE   161 AA;  17104 MW;  C8E2ED63D18C35AE CRC64;
     MSETIKVGIA DLKVGVAPQK IATIGLGSCV GVTLYDPVTK IGGMVHIMLP SSIEIKNSNN
     VAKFADTGVK KLLEDVLKKG CKKTNLIAKI VGGAQMFKLA TKDDTLRVGD KNIIAVKQIL
     RELDLSIRAS DVGGNYGRTI ILDLETGSLL VRTIGKGEKT I
//
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