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Database: UniProt
Entry: A0A1I6KYE9_9FIRM
LinkDB: A0A1I6KYE9_9FIRM
Original site: A0A1I6KYE9_9FIRM 
ID   A0A1I6KYE9_9FIRM        Unreviewed;       161 AA.
AC   A0A1I6KYE9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=SAMN05661086_02852 {ECO:0000313|EMBL:SFR95960.1};
OS   Anaeromicropila populeti.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaeromicropila.
OX   NCBI_TaxID=37658 {ECO:0000313|EMBL:SFR95960.1, ECO:0000313|Proteomes:UP000199659};
RN   [1] {ECO:0000313|EMBL:SFR95960.1, ECO:0000313|Proteomes:UP000199659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=743A {ECO:0000313|EMBL:SFR95960.1,
RC   ECO:0000313|Proteomes:UP000199659};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOYZ01000011; SFR95960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6KYE9; -.
DR   STRING; 37658.SAMN05661086_02852; -.
DR   OrthoDB; 9807202at2; -.
DR   Proteomes; UP000199659; 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; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR   PANTHER; PTHR35147:SF1; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR   Pfam; PF03975; CheD; 1.
DR   SUPFAM; SSF64438; CNF1/YfiH-like putative cysteine hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000199659}.
SQ   SEQUENCE   161 AA;  17294 MW;  BC57409531E0F61C CRC64;
     MGEMIRVGMA DLNICNSPNA ITTLGLGSCV GIILYDPIKK LAGLAHIMLP DSTKVKMNEN
     KAKFADTGTD LLLDLLLKAG AGKSNIVAKI AGGAQMFAFS SNNDMLRIGE RNVEATKEKL
     KLLGIRLLAQ DTGLNYGRTI EFYPETGELV IKAVGKEKKI I
//
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