CHED_XANCP
ID CHED_XANCP Reviewed; 198 AA.
AC Q8P9J6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=XCC1867;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM41156.1; -; Genomic_DNA.
DR RefSeq; NP_637232.1; NC_003902.1.
DR RefSeq; WP_011037037.1; NC_003902.1.
DR AlphaFoldDB; Q8P9J6; -.
DR SMR; Q8P9J6; -.
DR STRING; 340.xcc-b100_2155; -.
DR EnsemblBacteria; AAM41156; AAM41156; XCC1867.
DR GeneID; 58013584; -.
DR KEGG; xcc:XCC1867; -.
DR PATRIC; fig|190485.4.peg.1992; -.
DR eggNOG; COG1871; Bacteria.
DR HOGENOM; CLU_087854_0_0_6; -.
DR OMA; VGMADLN; -.
DR Proteomes; UP000001010; 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; Reference proteome.
FT CHAIN 1..198
FT /note="Probable chemoreceptor glutamine deamidase CheD"
FT /id="PRO_0000251080"
SQ SEQUENCE 198 AA; 21659 MW; 79D6CB612F022804 CRC64;
MSTAVQVDDV MRYRDSRFQT IAAKLLPTQY LVVDDDTALT TTLGSCVAAC LRDPVLKIGG
MNHFLLPEGQ VGDGAPARYG SYAMELLIND MLKRGAHRKR IEAKVFGGAN VLKGFTSNPV
GTRNAEFVRQ YLQAEHIPII AEDLCGIHPR KVWFFPTTGR VVVQRLPHAH EAEVAAAESA
VRARLSKAPV TGGVELFE