ID A0A2A2IG05_9BACI Unreviewed; 165 AA.
AC A0A2A2IG05;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CIL05_09100 {ECO:0000313|EMBL:PAV30023.1};
OS Virgibacillus profundi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=2024555 {ECO:0000313|EMBL:PAV30023.1, ECO:0000313|Proteomes:UP000218887};
RN [1] {ECO:0000313|EMBL:PAV30023.1, ECO:0000313|Proteomes:UP000218887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IO3-P3-H5 {ECO:0000313|EMBL:PAV30023.1,
RC ECO:0000313|Proteomes:UP000218887};
RA Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT moderately halophilic bacteria isolated from marine sediment by using the
RT Microfluidic Streak Plate.";
RL Submitted (AUG-2017) 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:PAV30023.1}.
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DR EMBL; NPOA01000005; PAV30023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2IG05; -.
DR OrthoDB; 9807202at2; -.
DR Proteomes; UP000218887; 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; 17741 MW; AB10E542CD5A2115 CRC64;
MNKTQTVISV GIADLNIVSA PNLIRTMGLG SCVGVVLYDS SKKIAGLSHV LLPDSSLTRQ
SSFNEYKYAD TAVPILVEKL VNAGAGKSRL KAKLAGGAQM FQFSSNSDII RIGPRNVEAV
QNILNKNHIP IISSDVGGNV GRTIEFDPVT SKLKIRKVNK EETFI
//