CHEB_ECOLI
ID CHEB_ECOLI Reviewed; 349 AA.
AC P07330; P78070;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000305};
DE EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:358191, ECO:0000269|PubMed:392505};
DE EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:6300110, ECO:0000269|PubMed:6304723};
DE AltName: Full=Chemotaxis response regulator protein-glutamate methylesterase/glutamine deamidase {ECO:0000305};
DE AltName: Full=Methyl-accepting chemotaxis proteins-specific methylesterase/deamidase {ECO:0000305};
DE Short=MCP-specific methylesterase/deamidase {ECO:0000305};
GN Name=cheB {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000303|PubMed:324984};
GN OrderedLocusNames=b1883, JW1872;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3510184; DOI=10.1128/jb.165.1.161-166.1986;
RA Mutoh N., Simon M.I.;
RT "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia
RT coli.";
RL J. Bacteriol. 165:161-166(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION, GENE NAME, AND FUNCTION.
RX PubMed=324984; DOI=10.1128/jb.130.3.1317-1325.1977;
RA Silverman M., Simon M.;
RT "Identification of polypeptides necessary for chemotaxis in Escherichia
RT coli.";
RL J. Bacteriol. 130:1317-1325(1977).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=353036; DOI=10.1128/jb.135.1.45-53.1978;
RA Parkinson J.S.;
RT "Complementation analysis and deletion mapping of Escherichia coli mutants
RT defective in chemotaxis.";
RL J. Bacteriol. 135:45-53(1978).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=358191; DOI=10.1073/pnas.75.8.3659;
RA Stock J.B., Koshland D.E. Jr.;
RT "A protein methylesterase involved in bacterial sensing.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:3659-3663(1978).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=392505; DOI=10.1073/pnas.76.11.5544;
RA Toews M.L., Goy M.F., Springer M.S., Adler J.;
RT "Attractants and repellents control demethylation of methylated chemotaxis
RT proteins in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:5544-5548(1979).
RN [9]
RP FUNCTION AS A DEAMIDASE.
RX PubMed=6300110; DOI=10.1016/s0021-9258(18)32536-5;
RA Kehry M.R., Engstrom P., Dahlquist F.W., Hazelbauer G.L.;
RT "Multiple covalent modifications of Trg, a sensory transducer of
RT Escherichia coli.";
RL J. Biol. Chem. 258:5050-5055(1983).
RN [10]
RP FUNCTION AS A DEAMIDASE.
RX PubMed=6304723; DOI=10.1073/pnas.80.12.3599;
RA Kehry M.R., Bond M.W., Hunkapiller M.W., Dahlquist F.W.;
RT "Enzymatic deamidation of methyl-accepting chemotaxis proteins in
RT Escherichia coli catalyzed by the cheB gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3599-3603(1983).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=3280143; DOI=10.1016/0092-8674(88)90489-8;
RA Hess J.F., Oosawa K., Kaplan N., Simon M.I.;
RT "Phosphorylation of three proteins in the signaling pathway of bacterial
RT chemotaxis.";
RL Cell 53:79-87(1988).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, PHOSPHORYLATION,
RP AND MUTAGENESIS OF ASP-10; ASP-11; ASP-56 AND LEU-99.
RX PubMed=2188960; DOI=10.1128/jb.172.6.3388-3399.1990;
RA Stewart R.C., Roth A.F., Dahlquist F.W.;
RT "Mutations that affect control of the methylesterase activity of CheB, a
RT component of the chemotaxis adaptation system in Escherichia coli.";
RL J. Bacteriol. 172:3388-3399(1990).
RN [13]
RP INTERACTION WITH CHEA.
RX PubMed=7578071; DOI=10.1021/bi00045a003;
RA Li J., Swanson R.V., Simon M.I., Weis R.M.;
RT "The response regulators CheB and CheY exhibit competitive binding to the
RT kinase CheA.";
RL Biochemistry 34:14626-14636(1995).
RN [14]
RP INTERACTION WITH CHEMORECEPTORS.
RX PubMed=16573695; DOI=10.1111/j.1365-2958.2006.05108.x;
RA Li M., Hazelbauer G.L.;
RT "The carboxyl-terminal linker is important for chemoreceptor function.";
RL Mol. Microbiol. 60:469-479(2006).
CC -!- FUNCTION: Involved in chemotaxis (PubMed:324984, PubMed:358191,
CC PubMed:392505, PubMed:2188960). Part of a chemotaxis signal
CC transduction system that modulates chemotaxis in response to various
CC stimuli (PubMed:392505, PubMed:2188960). Catalyzes the demethylation of
CC specific methylglutamate residues introduced into the chemoreceptors
CC (methyl-accepting chemotaxis proteins or MCP) by CheR (PubMed:358191,
CC PubMed:392505, PubMed:2188960). Also mediates the irreversible
CC deamidation of specific glutamine residues to glutamic acid
CC (PubMed:6300110, PubMed:6304723). Catalyzes its own deactivation by
CC removing the activating phosphoryl group (PubMed:2188960).
CC {ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:324984,
CC ECO:0000269|PubMed:358191, ECO:0000269|PubMed:392505,
CC ECO:0000269|PubMed:6300110, ECO:0000269|PubMed:6304723}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00099, ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:358191,
CC ECO:0000269|PubMed:392505};
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_00099, ECO:0000269|PubMed:6300110,
CC ECO:0000269|PubMed:6304723};
CC -!- ACTIVITY REGULATION: Methylesterase activity is activated via
CC phosphorylation in response to negative chemotactic stimuli and is
CC inhibited in the presence of attractants (PubMed:392505,
CC PubMed:2188960). Activation requires both CheA and CheW
CC (PubMed:2188960). {ECO:0000269|PubMed:2188960,
CC ECO:0000269|PubMed:392505}.
CC -!- SUBUNIT: Interacts with CheA (PubMed:7578071). Binds to a C-terminal
CC pentapeptide sequence carried by certain receptors (PubMed:16573695).
CC {ECO:0000269|PubMed:16573695, ECO:0000269|PubMed:7578071}.
CC -!- INTERACTION:
CC P07330; P07363: cheA; NbExp=3; IntAct=EBI-1125895, EBI-1026773;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099,
CC ECO:0000269|PubMed:358191}.
CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC region which modulates catalytic activity. {ECO:0000255|HAMAP-
CC Rule:MF_00099, ECO:0000269|PubMed:2188960}.
CC -!- PTM: Phosphorylated by CheA (PubMed:3280143, PubMed:2188960).
CC Phosphorylation of the N-terminal regulatory domain activates the
CC methylesterase activity (PubMed:2188960). {ECO:0000269|PubMed:2188960,
CC ECO:0000269|PubMed:3280143}.
CC -!- DISRUPTION PHENOTYPE: Mutants are defective in chemotaxis. They exhibit
CC very high tumbling rates. {ECO:0000269|PubMed:353036}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M13463; AAA23569.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74953.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15699.1; -; Genomic_DNA.
DR PIR; D25195; XYECEB.
DR RefSeq; NP_416397.1; NC_000913.3.
DR RefSeq; WP_000036361.1; NZ_LN832404.1.
DR AlphaFoldDB; P07330; -.
DR SMR; P07330; -.
DR BioGRID; 4260716; 222.
DR DIP; DIP-9272N; -.
DR IntAct; P07330; 10.
DR STRING; 511145.b1883; -.
DR PaxDb; P07330; -.
DR PRIDE; P07330; -.
DR EnsemblBacteria; AAC74953; AAC74953; b1883.
DR EnsemblBacteria; BAA15699; BAA15699; BAA15699.
DR GeneID; 946394; -.
DR KEGG; ecj:JW1872; -.
DR KEGG; eco:b1883; -.
DR PATRIC; fig|1411691.4.peg.364; -.
DR EchoBASE; EB0145; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_6; -.
DR InParanoid; P07330; -.
DR OMA; MLEMHRA; -.
DR PhylomeDB; P07330; -.
DR BioCyc; EcoCyc:CHEB-MON; -.
DR BioCyc; MetaCyc:CHEB-MON; -.
DR BRENDA; 3.1.1.61; 2026.
DR PRO; PR:P07330; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:1990827; F:deaminase binding; IDA:CAFA.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IDA:CAFA.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IDA:EcoCyc.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0018277; P:protein deamination; IDA:CAFA.
DR GO; GO:0006482; P:protein demethylation; IDA:CAFA.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR CDD; cd16432; CheB_Rec; 1.
DR Gene3D; 3.40.50.180; -; 1.
DR HAMAP; MF_00099; CheB_chemtxs; 1.
DR InterPro; IPR008248; CheB-like.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52738; SSF52738; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..349
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000157992"
FT DOMAIN 5..122
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 152..344
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 164
FT /evidence="ECO:0000250|UniProtKB:P04042, ECO:0000255|HAMAP-
FT Rule:MF_00099"
FT ACT_SITE 190
FT /evidence="ECO:0000250|UniProtKB:P04042, ECO:0000255|HAMAP-
FT Rule:MF_00099"
FT ACT_SITE 286
FT /evidence="ECO:0000250|UniProtKB:P04042, ECO:0000255|HAMAP-
FT Rule:MF_00099"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250|UniProtKB:P04042, ECO:0000255|HAMAP-
FT Rule:MF_00099"
FT MUTAGEN 10
FT /note="D->N: Eliminates activation in response to negative
FT stimuli, but does not affect response to positive stimuli."
FT /evidence="ECO:0000269|PubMed:2188960"
FT MUTAGEN 11
FT /note="D->E,N: Eliminates activation in response to
FT negative stimuli, but does not affect response to positive
FT stimuli."
FT /evidence="ECO:0000269|PubMed:2188960"
FT MUTAGEN 56
FT /note="D->E,N: Eliminates activation in response to
FT negative stimuli, but does not affect response to positive
FT stimuli."
FT /evidence="ECO:0000269|PubMed:2188960"
FT MUTAGEN 99
FT /note="L->P: Eliminates activation in response to negative
FT stimuli, but does not affect response to positive stimuli."
FT /evidence="ECO:0000269|PubMed:2188960"
FT CONFLICT 96
FT /note="A -> P (in Ref. 1; AAA23569)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="E -> Q (in Ref. 1; AAA23569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37468 MW; 6F3D1AFB8D23D3F5 CRC64;
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP DVLTLDVEMP
RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG AIDFVTKPQL GIREGMLAYN
EMIAEKVRTA AKASLAAHKP LSAPTTLKAG PLLSSEKLIA IGASTGGTEA IRHVLQPLPL
SSPALLITQH MPPGFTRSFA DRLNKLCQIG VKEAEDGERV LPGHAYIAPG DRHMELSRSG
ANYQIKIHDG PAVNRHRPSV DVLFHSVAKQ AGRNAVGVIL TGMGNDGAAG MLAMRQAGAW
TLAQNEASCV VFGMPREAIN MGGVCEVVDL SQVSQQMLAK ISAGQAIRI
