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Database: UniProt
Entry: A0A101G0W0_9ACTN
LinkDB: A0A101G0W0_9ACTN
Original site: A0A101G0W0_9ACTN 
ID   A0A101G0W0_9ACTN        Unreviewed;       355 AA.
AC   A0A101G0W0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=XD74_1427 {ECO:0000313|EMBL:KUK47989.1};
OS   Actinobacteria bacterium 66_15.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1635289 {ECO:0000313|EMBL:KUK47989.1, ECO:0000313|Proteomes:UP000057652};
RN   [1] {ECO:0000313|EMBL:KUK47989.1, ECO:0000313|Proteomes:UP000057652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=66_15 {ECO:0000313|EMBL:KUK47989.1};
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK47989.1}.
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DR   EMBL; LGFV01000038; KUK47989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101G0W0; -.
DR   PATRIC; fig|1635289.4.peg.1493; -.
DR   Proteomes; UP000057652; 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|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050};
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}.
FT   DOMAIN          11..129
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          166..348
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         62
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   355 AA;  37108 MW;  9FA8CB7F49D349EA CRC64;
     MPGTAEGQRI RVVIADDSIV AREMLAQILA SDPVIEVVGT ATNGEEAVDL VARLRPDLVT
     MDIHMPKMDG LEATERIMAF TPTPILVVSS SVYGEGMGRA FDALAVGALE VMKKPEPKDW
     ADLEAIGRQI IRTVKILSRV KVITHIRGRR APVHTGVPPV ESPDVGGDGL RIVAIGSSTG
     GPTALLEVLA RLPHDFPLPV VVAQHIADGF VPGLATWLDA ACKITVAAAA EGDVLQPGVA
     YLAATGTNME VDGRRLRFTK PQPGQLYIPS ADTLFESVAV SYAKKAVGVL LTGMGADGAR
     GLKALHDRGA PTICQDEATS TVWGMPKAAI DLGAARAVLP VHEIAGAIEG LLGDA
//
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