CHED_THEMA
ID CHED_THEMA Reviewed; 157 AA.
AC Q9X005;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Chemoreceptor glutamine deamidase CheD;
DE EC=3.5.1.44;
DE AltName: Full=Chemoreceptor glutamate methylesterase CheD;
DE EC=3.1.1.61;
GN Name=cheD; OrderedLocusNames=TM_0903;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHEC, AND MUTAGENESIS
RP OF THR-21; SER-26; CYS-27 AND HIS-44.
RX PubMed=16469702; DOI=10.1016/j.cell.2005.11.046;
RA Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W.,
RA Bilwes A.M., Crane B.R.;
RT "A receptor-modifying deamidase in complex with a signaling phosphatase
RT reveals reciprocal regulation.";
RL Cell 124:561-571(2006).
CC -!- FUNCTION: Deamidates glutamine residues on chemoreceptors (MCPs). CheD-
CC mediated MCP deamidation is required for productive communication of
CC the conformational signals of the chemoreceptors to the CheA kinase. In
CC addition, demethylates methylated glutamate residues on chemoreceptors
CC Mcp2 and Mcp4. Enhances the activity of CheC.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:82795; EC=3.1.1.61;
CC -!- SUBUNIT: Heterodimer with CheC. The CheC-CheD heterodimer interacts
CC with phosphorylated CheY. {ECO:0000269|PubMed:16469702}.
CC -!- SIMILARITY: Belongs to the CheD family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35984.1; -; Genomic_DNA.
DR PIR; F72318; F72318.
DR RefSeq; NP_228711.1; NC_000853.1.
DR RefSeq; WP_004080666.1; NZ_CP011107.1.
DR PDB; 2F9Z; X-ray; 2.40 A; C/D=1-157.
DR PDBsum; 2F9Z; -.
DR AlphaFoldDB; Q9X005; -.
DR SMR; Q9X005; -.
DR STRING; 243274.THEMA_00120; -.
DR EnsemblBacteria; AAD35984; AAD35984; TM_0903.
DR KEGG; tma:TM0903; -.
DR eggNOG; COG1871; Bacteria.
DR InParanoid; Q9X005; -.
DR OMA; VGMADLN; -.
DR OrthoDB; 1863047at2; -.
DR EvolutionaryTrace; Q9X005; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
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 3D-structure; Chemotaxis; Hydrolase; Reference proteome.
FT CHAIN 1..157
FT /note="Chemoreceptor glutamine deamidase CheD"
FT /id="PRO_0000251072"
FT ACT_SITE 27
FT /note="Nucleophile"
FT MUTAGEN 21
FT /note="T->A: 6-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16469702"
FT MUTAGEN 26
FT /note="S->A,H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16469702"
FT MUTAGEN 26
FT /note="S->N: Reduced activity."
FT /evidence="ECO:0000269|PubMed:16469702"
FT MUTAGEN 27
FT /note="C->A: Loss of activity. Does not prevent binding to
FT mcp2."
FT /evidence="ECO:0000269|PubMed:16469702"
FT MUTAGEN 27
FT /note="C->H,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16469702"
FT MUTAGEN 44
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16469702"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2F9Z"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2F9Z"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2F9Z"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2F9Z"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2F9Z"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2F9Z"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2F9Z"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2F9Z"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2F9Z"
SQ SEQUENCE 157 AA; 16657 MW; E5B03D96D2DDEDBE CRC64;
MKKVIGIGEY AVMKNPGVIV TLGLGSCVAV CMRDPVAKVG AMAHVMLPDS GGKTDKPGKY
ADTAVKTLVE ELKKMGAKVE RLEAKIAGGA SMFESKGMNI GARNVEAVKK HLKDFGIKLL
AEDTGGNRAR SVEYNIETGK LLVRKVGGGE QLEIKEI
