ID   CHED_BACSU              Reviewed;         166 AA.
AC   P40404;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Chemoreceptor glutamine deamidase CheD;
DE            EC=3.5.1.44;
GN   Name=cheD; Synonyms=ylxK; OrderedLocusNames=BSU16460;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2832368; DOI=10.1128/jb.170.4.1568-1574.1988;
RA   Helmann J.D., Marquez L.M., Chamberlin M.J.;
RT   "Cloning, sequencing, and disruption of the Bacillus subtilis sigma 28
RT   gene.";
RL   J. Bacteriol. 170:1568-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   ROLE IN CHEMOTAXIS, AND DISRUPTION PHENOTYPE.
RX   PubMed=7893679; DOI=10.1021/bi00011a040;
RA   Rosario M.M.L., Kirby J.R., Bochar D.A., Ordal G.W.;
RT   "Chemotactic methylation and behavior in Bacillus subtilis: role of two
RT   unique proteins, CheC and CheD.";
RL   Biochemistry 34:3823-3831(1995).
RN   [4]
RP   INTERACTION WITH CHEC.
RX   PubMed=8866475; DOI=10.1111/j.1365-2958.1996.tb02560.x;
RA   Rosario M.M.L., Ordal G.W.;
RT   "CheC and CheD interact to regulate methylation of Bacillus subtilis
RT   methyl-accepting chemotaxis proteins.";
RL   Mol. Microbiol. 21:511-518(1996).
RN   [5]
RP   FUNCTION IN DEAMIDATION OF MCPA; MCPB AND MCPC.
RX   PubMed=12011078; DOI=10.1074/jbc.m201334200;
RA   Kristich C.J., Ordal G.W.;
RT   "Bacillus subtilis CheD is a chemoreceptor modification enzyme required for
RT   chemotaxis.";
RL   J. Biol. Chem. 277:25356-25362(2002).
RN   [6]
RP   FUNCTION IN ACTIVATION OF CHEC.
RX   PubMed=14749334; DOI=10.1074/jbc.m311497200;
RA   Szurmant H., Muff T.J., Ordal G.W.;
RT   "Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-
RT   hydrolyzing proteins in the chemotactic signal transduction cascade.";
RL   J. Biol. Chem. 279:21787-21792(2004).
CC   -!- FUNCTION: Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA.
CC       In addition, deamidates other chemoreceptors, including McpB and McpC.
CC       CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is
CC       required for productive communication of the conformational signals of
CC       the chemoreceptors to the CheA kinase. CheD is absolutely required for
CC       a behavioral response mediated by McpC but is not required for the
CC       response to asparagine mediated by McpB. CheD is necessary for the
CC       generation of wild-type prestimulus CheA autophosphorylation levels.
CC       Also required for methylation of MCPs by CheR. In addition, enhances
CC       the activity of CheC 5-fold in vitro. {ECO:0000269|PubMed:12011078,
CC       ECO:0000269|PubMed:14749334, ECO:0000269|PubMed:7893679}.
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;
CC   -!- SUBUNIT: Forms a complex with CheC.
CC   -!- DISRUPTION PHENOTYPE: Cells exhibit poorly methylated receptors, are
CC       tumbly and have a decreased sensitivity to attractants.
CC       {ECO:0000269|PubMed:7893679}.
CC   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000305}.
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DR   EMBL; M20144; AAA61469.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13519.1; -; Genomic_DNA.
DR   PIR; B55216; B55216.
DR   RefSeq; NP_389528.1; NC_000964.3.
DR   RefSeq; WP_003244852.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P40404; -.
DR   SMR; P40404; -.
DR   IntAct; P40404; 3.
DR   STRING; 224308.BSU16460; -.
DR   PaxDb; P40404; -.
DR   PRIDE; P40404; -.
DR   EnsemblBacteria; CAB13519; CAB13519; BSU_16460.
DR   GeneID; 939959; -.
DR   KEGG; bsu:BSU16460; -.
DR   PATRIC; fig|224308.179.peg.1787; -.
DR   eggNOG; COG1871; Bacteria.
DR   InParanoid; P40404; -.
DR   OMA; VGMADLN; -.
DR   PhylomeDB; P40404; -.
DR   BioCyc; BSUB:BSU16460-MON; -.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
KW   Chemotaxis; Hydrolase; Reference proteome.
FT   CHAIN           1..166
FT                   /note="Chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_0000089639"
SQ   SEQUENCE   166 AA;  18008 MW;  3932F57E08C29ED8 CRC64;
     MSTTEAVVIK VGIADVKIAR FPDTIRTSGL GSCVGLVLYD KEKQTAGLVH VMLPDSTLSK
     TAELNRAKYA DTAVQTTIDM LIEAGCRKFA LKAKLAGGSE MFKFKSTNDL MKIGPRNVLA
     IKEQLSLFNI PIISEDTGGS SGRTIEFEPK SCMLHIRTVK QGEKTI