ID A0A4Z0H320_9BACI Unreviewed; 165 AA.
AC A0A4Z0H320;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 13.
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=E4663_07270 {ECO:0000313|EMBL:TGB04783.1};
OS Halobacillus salinus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Halobacillus.
OX NCBI_TaxID=192814 {ECO:0000313|EMBL:TGB04783.1, ECO:0000313|Proteomes:UP000297982};
RN [1] {ECO:0000313|EMBL:TGB04783.1, ECO:0000313|Proteomes:UP000297982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSL-3 {ECO:0000313|EMBL:TGB04783.1,
RC ECO:0000313|Proteomes:UP000297982};
RX PubMed=12807188; DOI=10.1099/ijs.0.02421-0;
RA Yoon J.H., Kang K.H., Park Y.H.;
RT "Halobacillus salinus sp. nov., isolated from a salt lake on the coast of
RT the East Sea in Korea.";
RL Int. J. Syst. Evol. Microbiol. 53:687-693(2003).
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}.
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:TGB04783.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SRJC01000001; TGB04783.1; -; Genomic_DNA.
DR RefSeq; WP_079480169.1; NZ_FVYZ01000004.1.
DR AlphaFoldDB; A0A4Z0H320; -.
DR STRING; 192814.GCA_900166575_01811; -.
DR OrthoDB; 9807202at2; -.
DR Proteomes; UP000297982; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000297982}.
SQ SEQUENCE 165 AA; 18112 MW; 0A21FEDE46DD26F1 CRC64;
MNEVLNIIKV GIADLKFVSA PDRIRTSGLG SCVGVVLFDP RKQLAGMAHV MLPDSHMAKQ
EKMNRFKYAD TALDDLLRGL TDNGASKFRM KAKIAGGAQM FSFKTSSDMM RIGPRNIEAV
KEKLAQFHIP IIAEDVGGKS GRTIVFDPST TDLHIRKVNH GEVTI
//
