ID A0A075JUK5_9BACI Unreviewed; 165 AA.
AC A0A075JUK5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 05-FEB-2025, entry version 33.
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=X953_11825 {ECO:0000313|EMBL:AIF43738.1};
OS Virgibacillus sp. SK37.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Virgibacillus.
OX NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF43738.1, ECO:0000313|Proteomes:UP000027985};
RN [1] {ECO:0000313|EMBL:AIF43738.1, ECO:0000313|Proteomes:UP000027985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK37 {ECO:0000313|EMBL:AIF43738.1,
RC ECO:0000313|Proteomes:UP000027985};
RA Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT halophilic bacterium isolated from Thai fish sauce fermentation.";
RL Submitted (FEB-2014) 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=L-glutaminyl-[protein] + H2O = 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; CP007161; AIF43738.1; -; Genomic_DNA.
DR RefSeq; WP_040955648.1; NZ_CP007161.1.
DR AlphaFoldDB; A0A075JUK5; -.
DR STRING; 403957.X953_11825; -.
DR KEGG; vir:X953_11825; -.
DR HOGENOM; CLU_087854_2_0_9; -.
DR OrthoDB; 9807202at2; -.
DR Proteomes; UP000027985; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027985}.
SQ SEQUENCE 165 AA; 17876 MW; FC557D43742D67B9 CRC64;
MNDVQTVVKV GIADLNAIMA PDLIRTAGLG SCVGVVMYDQ TNQIAGLSHI LLPDSSLAKQ
ENINKYKYAD TAIPLLLEKM LELGARKSAV KAKIAGGAQM FQFSSNTDIM RIGPRNSDAV
IEMLKKLRIP VIASDIGGNS GRTIEFDPTT SKLKIRKVNK AEIYI
//