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Database: UniProt
Entry: A0A075JUK5_9BACI
LinkDB: A0A075JUK5_9BACI
Original site: A0A075JUK5_9BACI 
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
//
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