ID B3PFF7_CELJU Unreviewed; 299 AA.
AC B3PFF7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN Name=cheB {ECO:0000313|EMBL:ACE83975.1};
GN OrderedLocusNames=CJA_0073 {ECO:0000313|EMBL:ACE83975.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE83975.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE83975.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE83975.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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};
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DR EMBL; CP000934; ACE83975.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PFF7; -.
DR STRING; 498211.CJA_0073; -.
DR KEGG; cja:CJA_0073; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_064504_0_0_6; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
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 SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Reference proteome {ECO:0000313|Proteomes:UP000001036}.
FT DOMAIN 110..299
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 299 AA; 32692 MW; 45D8C62E68C1F292 CRC64;
MGIVVDSAAK QQALAQLVAQ SGHQLCCQLL IKTDTEALPH PLLDAWLVDV AQDYPDDHHL
FEQLFNDSRI PVIVSDSDEY PINSEEYRAC LRRTAQRLRR LSSDINLQQA TPARDLWILG
ASTGGPAAVK RFLSRLPDNL GVAFLYVQHI DHQQTAPLNR MMNSAGGYPA MVASPGMVLE
PNRLILVTAL DRVEILDNRT LAVSHGEGWK GNYAPSIDQM CANAARVYRQ HCGLIIFTGM
GDDGAASCRL IKQLGGQVWV QTPTECTSDS MPLSALATGC VGYIGSPEAL AHTLTQQYR
//
