CHEB3_RHOPB
ID CHEB3_RHOPB Reviewed; 364 AA.
AC Q20XE6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase 3 {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};
GN Name=cheB3 {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=RPC_4668;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00099}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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 -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD90190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000301; ABD90190.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041802228.1; NC_007925.1.
DR AlphaFoldDB; Q20XE6; -.
DR SMR; Q20XE6; -.
DR STRING; 316056.RPC_4668; -.
DR PRIDE; Q20XE6; -.
DR EnsemblBacteria; ABD90190; ABD90190; RPC_4668.
DR KEGG; rpc:RPC_4668; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_5; -.
DR OrthoDB; 1655418at2; -.
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 GO; GO:0018277; P:protein deamination; IEA:UniProtKB-UniRule.
DR GO; GO:0006482; P:protein demethylation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein.
FT CHAIN 1..364
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase 3"
FT /id="PRO_0000264308"
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 167..358
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 178
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 204
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 300
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 364 AA; 39539 MW; CB9FD2A56514E4D8 CRC64;
MLRPKIRVLI VDDSASVRQI LTTILNADPD IEVMASAADP FAAARRLQDE IPDVIILDIE
MPRMDGITFL RKIMAQRPIP VIICSTLTEE RSDVMFEAFE AGAFDIVPKP RIDTTHALLE
ASARMCDAVK AAARARIRPR RPPRMVVEAK LTADAIMPPP VSGRARPTTE RLVCIGVSTG
GTEALRDVLE CLPAKAPAIL IVQHMPQGFT AAFAKRLDSL CEIEVREAQD GDVVVQGCAY
IAPGGRHMLL QRTGQRYHIA IKDGPPVSRH RPSADVLFRS AAQYAGPNAL GIIMTGMGDD
GARGLLEMHK LGATTRAQDE ESCVVFGMPK EAIALGGVDK VVPLAQIPRE IMLWQDAKQP
VPTV
