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Database: UniProt
Entry: J3JGQ2_9EURY
LinkDB: J3JGQ2_9EURY
Original site: J3JGQ2_9EURY 
ID   J3JGQ2_9EURY            Unreviewed;       161 AA.
AC   J3JGQ2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=HSB1_08940 {ECO:0000313|EMBL:EJN60291.1};
OS   Halogranum salarium B-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN60291.1, ECO:0000313|Proteomes:UP000007813};
RN   [1] {ECO:0000313|EMBL:EJN60291.1, ECO:0000313|Proteomes:UP000007813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-1 {ECO:0000313|EMBL:EJN60291.1,
RC   ECO:0000313|Proteomes:UP000007813};
RX   PubMed=23144405; DOI=10.1128/JB.01815-12;
RA   Kim K.K., Lee K.C., Lee J.S.;
RT   "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT   salarium B-1T.";
RL   J. Bacteriol. 194:6659-6659(2012).
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:EJN60291.1}.
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DR   EMBL; ALJD01000003; EJN60291.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3JGQ2; -.
DR   PATRIC; fig|1210908.3.peg.849; -.
DR   eggNOG; arCOG02380; Archaea.
DR   Proteomes; UP000007813; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   161 AA;  16569 MW;  547AE8918C7DB665 CRC64;
     MSRNTPPRTR VGIADYAVTT TSGVLSTSGL GSCLCIVLVD ESTTVAGLLH AMLPEATPEH
     TSPAKFVDTG IEAMLTAMRE AGATPTGVTA KIVGGSTMLE LTSTDGSIGE RNVDATRTAL
     GALGIPIVAE DVGGTHGRSV RFDVETGDLR VKTAYHGEQI L
//
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