CHED_BORPA
ID CHED_BORPA Reviewed; 212 AA.
AC Q7W3Q2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=BPP3978;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
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DR EMBL; BX640435; CAE39261.1; -; Genomic_DNA.
DR RefSeq; WP_010929328.1; NC_002928.3.
DR AlphaFoldDB; Q7W3Q2; -.
DR SMR; Q7W3Q2; -.
DR EnsemblBacteria; CAE39261; CAE39261; BPP3978.
DR KEGG; bpa:BPP3978; -.
DR HOGENOM; CLU_087854_0_0_4; -.
DR OMA; VGMADLN; -.
DR Proteomes; UP000001421; 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; PTHR35147; 1.
DR Pfam; PF03975; CheD; 1.
DR SUPFAM; SSF64438; SSF64438; 1.
PE 3: Inferred from homology;
KW Chemotaxis; Hydrolase.
FT CHAIN 1..212
FT /note="Probable chemoreceptor glutamine deamidase CheD"
FT /id="PRO_0000251008"
SQ SEQUENCE 212 AA; 23148 MW; C95169870F97971C CRC64;
MPARLDARAT RRYFDSAFNS PAVKILPNEY YVTNGEDVML STVLGSCVAA CIHDPVIGVG
GMNHFMLPEG DIHSPASATM RYGAFAMEVL INELLKAGAV RERLEAKVFG GGAVLSAMQL
MNIGERNGQF VLNYLKTEGI PVRAQDLGDV HARRINYFPR DGRVMVRKMA PHHQKAEALI
AQREAAAAQT VQAETRAAPR VERFARPGGM PV