ID Q48II4_PSE14 Unreviewed; 204 AA.
AC Q48II4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN Name=cheB2 {ECO:0000313|EMBL:AAZ34670.1};
GN OrderedLocusNames=PSPPH_2603 {ECO:0000313|EMBL:AAZ34670.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ34670.1, ECO:0000313|Proteomes:UP000000551};
RN [1] {ECO:0000313|EMBL:AAZ34670.1, ECO:0000313|Proteomes:UP000000551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ34670.1; -; Genomic_DNA.
DR RefSeq; WP_004658106.1; NC_005773.3.
DR AlphaFoldDB; Q48II4; -.
DR KEGG; psp:PSPPH_2603; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_2_6; -.
DR Proteomes; UP000000551; 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 CDD; cd16433; CheB; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}.
FT DOMAIN 13..198
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 25
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 204 AA; 21949 MW; 63ADD95DEABC0772 CRC64;
MRTTFDDDLS CGPLPVVDAI VLGASAGGVE ALLKIFRNLR PGFSLPILMV LHLPDDRRSQ
LAHVFQNRLA IPVKEADDKE DIVPGTLYVA PAGYHVSVES DFSLSLSQED RVFYSRPSID
ILFGSAADAY GPRLAGVLLT GANNDGAQGL LQIKKYGGFT VIQDPSQAQA STMPQAGLVL
HSPDYLLSLN DIGRLLVELE RTAC
//
