ID A0A1R0WTT7_9BACL Unreviewed; 165 AA.
AC A0A1R0WTT7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BSO21_24160 {ECO:0000313|EMBL:OMD20920.1};
OS Paenibacillus odorifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=189426 {ECO:0000313|EMBL:OMD20920.1, ECO:0000313|Proteomes:UP000187158};
RN [1] {ECO:0000313|EMBL:OMD20920.1, ECO:0000313|Proteomes:UP000187158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0433 {ECO:0000313|EMBL:OMD20920.1,
RC ECO:0000313|Proteomes:UP000187158};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-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:OMD20920.1}.
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DR EMBL; MPVP01000211; OMD20920.1; -; Genomic_DNA.
DR RefSeq; WP_076219965.1; NZ_MPVP01000211.1.
DR AlphaFoldDB; A0A1R0WTT7; -.
DR STRING; 189426.PODO_18345; -.
DR eggNOG; COG1871; Bacteria.
DR Proteomes; UP000187158; 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.
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}.
SQ SEQUENCE 165 AA; 17450 MW; FCEFF9233E628CBF CRC64;
MIEEQSIIKV GMADLNVGSQ DSLIRTTGLG SCVGLTLFDP GKKLAGMAHV MLPSSEIARE
GQLNIAKFAD TAVPELLSRL LELGAVRSRI VAKMAGGSQM FAFAGGSDTM RIGPRNVESC
KLALENLKIP LIAEDTGGNY GRTIEIACNT GVLFIRSVQK GAKEL
//
