ID   CHED_BORAP              Reviewed;         163 AA.
AC   Q0SMQ0; G0IQF7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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};
GN   OrderedLocusNames=BAPKO_0639, BafPKo_0623;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01878.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69827.1; -; Genomic_DNA.
DR   RefSeq; WP_004789631.1; NC_017238.1.
DR   AlphaFoldDB; Q0SMQ0; -.
DR   SMR; Q0SMQ0; -.
DR   STRING; 390236.BafPKo_0623; -.
DR   EnsemblBacteria; AEL69827; AEL69827; BafPKo_0623.
DR   KEGG; baf:BAPKO_0639; -.
DR   KEGG; bafz:BafPKo_0623; -.
DR   PATRIC; fig|390236.22.peg.600; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_0_12; -.
DR   OMA; VGMADLN; -.
DR   OrthoDB; 1863047at2; -.
DR   Proteomes; UP000005216; 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..163
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_1000068543"
SQ   SEQUENCE   163 AA;  18084 MW;  7C7D88F65FD40697 CRC64;
     MLNHFNFKLK RDVTIIVPGE AFVSNKRVIS TILGSCVAVV LCDESSNLIG MNHYVLVKSD
     LDISPAQRGR YGIYAIPMLI NAMLENGANK SNLKAKLFGG TNFMAKGSVK VGLENSEFAI
     NTLNKYRIPI LAKDFDQSKS RKIFAFPESF KVIVEYPDGT KVF