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Database: UniProt
Entry: I3V0A8_PSEPU
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Original site: I3V0A8_PSEPU 
ID   I3V0A8_PSEPU            Unreviewed;       372 AA.
AC   I3V0A8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=YSA_08153 {ECO:0000313|EMBL:AFK71179.1};
OS   Pseudomonas putida ND6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK71179.1, ECO:0000313|Proteomes:UP000005268};
RN   [1] {ECO:0000313|EMBL:AFK71179.1, ECO:0000313|Proteomes:UP000005268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND6 {ECO:0000313|EMBL:AFK71179.1,
RC   ECO:0000313|Proteomes:UP000005268};
RX   PubMed=22933774; DOI=10.1128/JB.01190-12;
RA   Li S., Zhao H., Li Y., Niu S., Cai B.;
RT   "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT   Strain ND6.";
RL   J. Bacteriol. 194:5154-5155(2012).
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}.
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DR   EMBL; CP003588; AFK71179.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3V0A8; -.
DR   KEGG; ppi:YSA_08153; -.
DR   PATRIC; fig|231023.4.peg.3920; -.
DR   HOGENOM; CLU_000445_51_0_6; -.
DR   Proteomes; UP000005268; 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:SF3; 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}; Cytoplasm {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          6..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          181..369
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   REGION          152..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   372 AA;  39744 MW;  B5514B71A9D7CE51 CRC64;
     MFMAVKVLVV DDSGFFRRRV SEILSADPTI QVVGTATNGK EAIDQALALK PDVITMDYEM
     PMMDGITAVR HIMQRCPTPV LMFSSLTHEG ARVTLDALDA GAVDYLPKNF EDISRNPDKV
     KQLLCEKVHT ISRSNRRIGS YARTAPVATP APASTFASQA QTRPAAPARA AAPTPAASQS
     PAPKRKPYKL VAIGTSTGGP VALQRVLTQL PANFPAPIVL IQHMPAAFTK AFAERLDKLC
     RISVKEAEDG DMLRPGLALL APGGKQMMID GRGTVKILPG DERLNYKPCV DITFGSAAKS
     YGDKVLSVVL TGMGADGREG ARLLKQGGST VWAQDEASCV IYGMPMAIVK ANLADAVYSL
     DEIGKHLVEA CI
//
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