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
//