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Database: UniProt
Entry: A0A1C3EJ08_9GAMM
LinkDB: A0A1C3EJ08_9GAMM
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ID   A0A1C3EJ08_9GAMM        Unreviewed;       353 AA.
AC   A0A1C3EJ08;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000256|HAMAP-Rule:MF_00099};
DE            EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099};
DE            EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_00099};
GN   Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN   ORFNames=A8L45_11170 {ECO:0000313|EMBL:ODA33231.1};
OS   Veronia pacifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Veronia.
OX   NCBI_TaxID=1080227 {ECO:0000313|EMBL:ODA33231.1, ECO:0000313|Proteomes:UP000094936};
RN   [1] {ECO:0000313|EMBL:ODA33231.1, ECO:0000313|Proteomes:UP000094936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 1920 {ECO:0000313|EMBL:ODA33231.1,
RC   ECO:0000313|Proteomes:UP000094936};
RA   Gomez-Gil B., Enciso-Ibarra J.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (MAY-2016) 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:0000256|HAMAP-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:0000256|HAMAP-
CC         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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000941, ECO:0000256|HAMAP-
CC         Rule:MF_00099};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}.
CC   -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC       region which modulates catalytic activity. {ECO:0000256|HAMAP-
CC       Rule:MF_00099}.
CC   -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC       regulatory domain activates the methylesterase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00099}.
CC   -!- SIMILARITY: Belongs to the CheB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00099}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODA33231.1}.
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DR   EMBL; LYBM01000018; ODA33231.1; -; Genomic_DNA.
DR   RefSeq; WP_068902351.1; NZ_LYBM01000018.1.
DR   AlphaFoldDB; A0A1C3EJ08; -.
DR   STRING; 1080227.A8L45_11170; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000094936; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW   Rule:MF_00099};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00099};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000094936}.
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          160..353
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   353 AA;  38777 MW;  3EB35285E7BE4504 CRC64;
     MKKRRIKVLV VDDSAVFRAL LTDILESDPQ LKVVAGAEDP YEARELIKKL KPDVLTLDVE
     MPRMDGVQFL RNLMRLHPLP VVMLSTLTQH KADVTLASLE IGAVDYLPKP TKNLQSELES
     YREVLIEKVK MAAKANLTAH AEIMSGPSYS KIDISAQRFD ASLVDVIAIG ASTGGTEALK
     VLLKNMPAKM PPIVITQHIK AVFSKSFADR LNRESALHVE ELTNKQSPLI PGRVYVAPGD
     KHIEVIKKGQ RFYCRQNDGD PVLRHKPSVD VMFQSVVKAA GGRAVGILLT GMGRDGADGM
     KAMHTAGAVT LAQDELTSVV WGMPRVAIEM GAATHVMPLK KITPFLVEMF YHS
//
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