ID A0A024HCH5_PSEKB Unreviewed; 352 AA.
AC A0A024HCH5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=cheB2 {ECO:0000313|EMBL:CDF82168.1};
GN Synonyms=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN ORFNames=PKB_0800 {ECO:0000313|EMBL:CDF82168.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF82168.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF82168.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF82168.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF82168.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF82168.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG322950; CDF82168.1; -; Genomic_DNA.
DR RefSeq; WP_043249194.1; NZ_HG322950.1.
DR AlphaFoldDB; A0A024HCH5; -.
DR STRING; 1301098.PKB_0800; -.
DR KEGG; pkc:PKB_0800; -.
DR PATRIC; fig|1301098.3.peg.803; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_6; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000025241; 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: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:UP000025241}.
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 163..352
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 175
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 201
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 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 352 AA; 38071 MW; 62DAFFDB47238770 CRC64;
MSIKVMIVDD SAVMREVMQQ MLQGYADIEV IGAAMDPLLA LQKMERAWPD VILLDVEMPR
MDGITFLRQI MSTRPTPVVI CSTLTEKGAD ITLQALAAGA VEVICKPTSG LRDFLQASVQ
ELVGAIRTAA RARARPSAPM PAPEFKRSAD ALLSLPGNAL LNQRTTERIV VMGTSTGGTQ
ALEHVLCQLP LNAPGIAIVQ HMPEKFTRSF AQRLDSLCAI EVREAQDGDR ILPGRALIAP
GGRHLLVRRS GAQYLVEVRD GPLVSRHRPS VDVLFRSAAV HAGRNALGVI MTGMGDDGAR
GLKEMHEAGA RTCAQDEDSC VVFGMPKEAI RLGGVDQVVS LERIAQVVTE WR
//
