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CHEB3_GEOSL
ID   CHEB3_GEOSL             Reviewed;         371 AA.
AC   P62640; Q74AY5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=GSU2214;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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}.
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DR   EMBL; AE017180; AAR35590.1; -; Genomic_DNA.
DR   RefSeq; NP_953263.1; NC_002939.5.
DR   RefSeq; WP_010942854.1; NC_002939.5.
DR   AlphaFoldDB; P62640; -.
DR   SMR; P62640; -.
DR   STRING; 243231.GSU2214; -.
DR   EnsemblBacteria; AAR35590; AAR35590; GSU2214.
DR   KEGG; gsu:GSU2214; -.
DR   PATRIC; fig|243231.5.peg.2245; -.
DR   eggNOG; COG2201; Bacteria.
DR   HOGENOM; CLU_000445_51_0_7; -.
DR   InParanoid; P62640; -.
DR   OMA; ISQHMPA; -.
DR   Proteomes; UP000000577; 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   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; Reference proteome.
FT   CHAIN           1..371
FT                   /note="Protein-glutamate methylesterase/protein-glutamine
FT                   glutaminase 3"
FT                   /id="PRO_0000157998"
FT   DOMAIN          5..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   DOMAIN          174..362
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ   SEQUENCE   371 AA;  39996 MW;  1297ADD7443D47A7 CRC64;
     MRKIRVVVID DSAYSRRAIT KMLESMPEVE VIGYATDGEE GIRKIIDLKP DLVTLDLEMP
     RMDGFTLLRI VMEYSPTAVI VISSRSEDEK VFRALELGAV DFVAKPTKGV SEEILTIRED
     LHRKVRGVIH LNLAGIVRRE REQERASVAA GRRTSGSAPY AKAAVRTEST APRPAGRLEV
     VAIGASTGGP PALQRILCAL PGAFPQAVVV SQHMPAGFTR TFAERLNRLS PLEICEAADG
     DEVRAGRVLI APGGHNMVFE RQGSEVRARI VKPGTDDRYV PSVDAMLLSC AEVFGPRTLG
     VVLTGMGNDG SKGVAAINRA GGQTLAEAEE TAVVFGMPKE AIATGVVDKI VSLDRMSREI
     IQRCGLLSDV D
 
 
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