CHED_RALPJ
ID CHED_RALPJ Reviewed; 236 AA.
AC B2UHV5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000255|HAMAP-Rule:MF_01440};
DE EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN Name=cheD {ECO:0000255|HAMAP-Rule:MF_01440}; OrderedLocusNames=Rpic_4053;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_01440};
CC -!- SIMILARITY: Belongs to the CheD family. {ECO:0000255|HAMAP-
CC Rule:MF_01440}.
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; CP001069; ACD29156.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UHV5; -.
DR SMR; B2UHV5; -.
DR STRING; 402626.Rpic_4053; -.
DR EnsemblBacteria; ACD29156; ACD29156; Rpic_4053.
DR KEGG; rpi:Rpic_4053; -.
DR eggNOG; COG1871; Bacteria.
DR HOGENOM; CLU_087854_0_0_4; -.
DR OMA; VGMADLN; -.
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; PTHR35147; 1.
DR Pfam; PF03975; CheD; 1.
DR SUPFAM; SSF64438; SSF64438; 1.
PE 3: Inferred from homology;
KW Chemotaxis; Hydrolase.
FT CHAIN 1..236
FT /note="Probable chemoreceptor glutamine deamidase CheD"
FT /id="PRO_1000145892"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 236 AA; 25446 MW; 6930C1260782272F CRC64;
MIEFGKRATP QSAADAVRGD SGMASGMSAG AMATLAQSAA STHAYYDTTF SRRAMKVLPG
EYSVTTEDLM LVTVLGSCVS ACVRDKTLGI GGMNHFMLPS RNEGESILSP SMRYGTHAME
VLLNQLYKAG AKRERLEIKV FGGAAVLAGM STLDVGERNG KFVLEFLRNE GLTVAAKDLF
DVHPRKVYFV PSTGQIMVRK LRSQNSAAEL DSEAQYASKL SKSITTKPAS RLQLFT