ID CHEB_PECAS Reviewed; 350 AA.
AC Q6D6I7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000255|HAMAP-Rule:MF_00099};
DE EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099};
DE EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_00099};
DE AltName: Full=CheB_Pec {ECO:0000303|PubMed:33187094};
GN Name=cheB {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=ECA1693;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2] {ECO:0007744|PDB:6YMZ}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=33187094; DOI=10.3390/ijms21228459;
RA Velando F., Gavira J.A., Rico-Jimenez M., Matilla M.A., Krell T.;
RT "Evidence for pentapeptide-dependent and independent CheB
RT methylesterases.";
RL Int. J. Mol. Sci. 21:0-0(2020).
CC -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC transduction system that modulates chemotaxis in response to various
CC stimuli. Catalyzes the demethylation of specific methylglutamate
CC residues introduced into the chemoreceptors (methyl-accepting
CC chemotaxis proteins or MCP) by CheR. Also mediates the irreversible
CC deamidation of specific glutamine residues to glutamic acid (By
CC similarity). Does not interact with the C-terminal pentapeptide of the
CC chemoreceptors (PubMed:33187094). {ECO:0000255|HAMAP-Rule:MF_00099,
CC ECO:0000269|PubMed:33187094}.
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};
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099}.
CC -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC region which modulates catalytic activity. Domains are connected by a
CC linker of approximately 25 amino acids (PubMed:33187094). The
CC structural disorder in the region homologous to the pentapeptide-
CC binding site in E.coli may be related to the failure to bind
CC pentapeptides (PubMed:33187094). {ECO:0000269|PubMed:33187094}.
CC -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC regulatory domain activates the methylesterase activity.
CC {ECO:0000255|HAMAP-Rule:MF_00099}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not mediate chemotaxis towards
CC casamino acids. {ECO:0000269|PubMed:33187094}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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DR EMBL; BX950851; CAG74599.1; -; Genomic_DNA.
DR RefSeq; WP_011093272.1; NC_004547.2.
DR PDB; 6YMZ; X-ray; 2.30 A; A/B/C/D/E=1-350.
DR PDBsum; 6YMZ; -.
DR AlphaFoldDB; Q6D6I7; -.
DR SMR; Q6D6I7; -.
DR STRING; 218491.ECA1693; -.
DR GeneID; 57209594; -.
DR KEGG; eca:ECA1693; -.
DR PATRIC; fig|218491.5.peg.1720; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_6; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR CDD; cd17541; REC_CheB-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 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 PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR PANTHER; PTHR42872:SF6; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE; 1.
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; CheY-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..350
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000225460"
FT DOMAIN 5..122
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 153..345
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 191
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:6YMZ"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6YMZ"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:6YMZ"
SQ SEQUENCE 350 AA; 37998 MW; D44548BA0F7AD6CB CRC64;
MSKIRVLCVD DSALMRQIMT EIINSHPDME VVATAPDPLV ARDLIKKFNP QVLTLDVEMP
RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EITLRALELG AIDFVTKPQL GIREGMLAYS
ELIAEKIRMA AKARLPQRST TAEPTKIIQH MPLLSSEKLI AIGASTGGTE AIRHVLQPLP
PTSPALLITQ HMPPGFTKSF AERLNKLCQI TVKEAEDGER VLPGHAYIAP GARHLELARS
GANYQVRLND GPPVNRHRPS VDVLFRSVAQ YAGRNAVGVI LTGMGNDGAA GMLELHQAGA
YTLAQNEASC VVFGMPREAI AMGGVDEVVD LHQVSQRMLA QISAGQALRI
//
