ID W0JNI7_9EURY Unreviewed; 244 AA.
AC W0JNI7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 02-APR-2025, entry version 35.
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=HALLA_16550 {ECO:0000313|EMBL:AHG00169.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG00169.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHG00169.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHG00169.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-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; CP007055; AHG00169.1; -; Genomic_DNA.
DR AlphaFoldDB; W0JNI7; -.
DR STRING; 797299.HALLA_16550; -.
DR KEGG; hlr:HALLA_16550; -.
DR PATRIC; fig|797299.3.peg.2316; -.
DR eggNOG; arCOG02380; Archaea.
DR HOGENOM; CLU_1136026_0_0_2; -.
DR Proteomes; UP000019024; 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:UP000019024}.
FT REGION 17..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 244 AA; 25648 MW; 83710CBEDA8740DF CRC64;
MIQMTDDLLD RADGFESHEV SVCRTETSPS RSRSNRRSSA TTFDSKTPSP KAVHPGSNDP
VTIHQAARVE SPTVVPGPDD SLEESAFKVG IAEYALTVRN EYQMLRSSGF GSCIGVVLHD
ESAAITGLLH FMLPATEEIA NSDPNPAKFG DSGIEAMLDS FREVGGSNST TTAKLAGGAA
MMDFGDDGDS IGKQNTVAAR TALQDHDIPI TAAETGGSVG RSVTVDAQTA SVTIQRSDGS
ERVI
//
